Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
ABC-type (ATP-binding cassette) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that exports lipo-oligosaccharides of gram negative bacteria
-
-
-
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
LptB2FG tetramer mechanism: 1. Resting: the LptB nucleotide-binding sites are unoccupied, and the LptF/G cavity is oriented inwards. 2. Open: ATP binds LptB, inducing the LptF/G cavity to open away from the IM, and receives the Lipid A moiety of LPS, which is still embedded in the IM. 3. Close: LptB hydrolyzes ATP, inducing the LptF/G cavity to close again. LPS is forced out of the IM into the periplasm
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
LptB2FG tetramer mechanism: 1. Resting: the LptB nucleotide-binding sites are unoccupied, and the LptF/G cavity is oriented inwards. 2. Open: ATP binds LptB, inducing the LptF/G cavity to open away from the IM, and receives the Lipid A moiety of LPS, which is still embedded in the IM. 3. Close: LptB hydrolyzes ATP, inducing the LptF/G cavity to close again. LPS is forced out of the IM into the periplasm
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
LptB2FG tetramer mechanism: 1. Resting: the LptB nucleotide-binding sites are unoccupied, and the LptF/G cavity is oriented inwards. 2. Open: ATP binds LptB, inducing the LptF/G cavity to open away from the IM, and receives the Lipid A moiety of LPS, which is still embedded in the IM. 3. Close: LptB hydrolyzes ATP, inducing the LptF/G cavity to close again. LPS is forced out of the IM into the periplasm
Neisseria meningitidis serogroup B / serotype 15
ATP + H2O + lipopolysaccharide[side 1] = ADP + phosphate + lipopolysaccharide[side 2]
LptB2FG tetramer mechanism: 1. Resting: the LptB nucleotide-binding sites are unoccupied, and the LptF/G cavity is oriented inwards. 2. Open: ATP binds LptB, inducing the LptF/G cavity to open away from the IM, and receives the Lipid A moiety of LPS, which is still embedded in the IM. 3. Close: LptB hydrolyzes ATP, inducing the LptF/G cavity to close again. LPS is forced out of the IM into the periplasm
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
ATP + H2O + lipopolysaccharide/in
ADP + phosphate + lipopolysaccharide/out
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
additional information
?
-
ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
-
Substrates: -
Products: -
?
ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
-
Substrates: translocation of the lipid A core moiety across the inner membrane requires the ABC transporter MsbA,which mediates the flipping from the inner leaflet to the outer leaflet of the inner membrane, lipopolysaccharide translocation mechanism and system, structure modelling, overview
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Neisseria meningitidis serogroup B / serotype 15
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Neisseria meningitidis serogroup B / serotype 15 H44/76
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Substrates: -
Products: -
?
additional information
?
-
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Substrates: ATPase assays are conducted for both LptB and LptB2FGC variants
Products: -
?
additional information
?
-
Neisseria meningitidis serogroup B / serotype 15
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Neisseria meningitidis serogroup B / serotype 15 H44/76
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + Lipid A/in
ADP + phosphate + Lipid A/out
-
Substrates: translocation of the lipid A core moiety across the inner membrane requires the ABC transporter MsbA,which mediates the flipping from the inner leaflet to the outer leaflet of the inner membrane, lipopolysaccharide translocation mechanism and system, structure modelling, overview
Products: -
?
ATP + H2O + lipopolysaccharide/in
ADP + phosphate + lipopolysaccharide/out
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
additional information
?
-
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Neisseria meningitidis serogroup B / serotype 15
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Neisseria meningitidis serogroup B / serotype 15 H44/76
Substrates: -
Products: -
?
ATP + H2O + lipopolysaccharide[side 1]
ADP + phosphate + lipopolysaccharide[side 2]
Substrates: -
Products: -
?
additional information
?
-
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Neisseria meningitidis serogroup B / serotype 15
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Neisseria meningitidis serogroup B / serotype 15 H44/76
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
additional information
?
-
Substrates: the Lpt (LPS transport) system forms a continuous protein bridge across the inner membrane, periplasm and outer membrane. LptB, LptG, and LptF extract LPS (lipopolysaccharide) from the inner leaflet of the IM (inner membrane) through an ATPase-dependent mechanism
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
LptB2FG represents a third distinct type of ABC transporter, deemed type-III
evolution
LptB2FG represents a third distinct type of ABC transporter, deemed type-III
evolution
Neisseria meningitidis serogroup B / serotype 15
LptB2FG represents a third distinct type of ABC transporter, deemed type-III
evolution
Neisseria meningitidis serogroup B / serotype 15
the Lpt system does not function in a completely conserved manner in all Gram-negative bacteria
evolution
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
LptB2FG represents a third distinct type of ABC transporter, deemed type-III
-
evolution
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
the Lpt system does not function in a completely conserved manner in all Gram-negative bacteria
-
malfunction
mutations in the nucleotide-binding domain, LptB, of the transporter inactivates transporter function in vivo
malfunction
the C-term LptC mutation reduces the stability of the overall LptB2FGC complex, so increased LptB expression compensates by shifting the binding equilibrium in favor of the LptB2FG complex
malfunction
the C-term LptC mutation reduces the stability of the overall LptB2FGC complex, so increased LptB expression compensates by shifting the binding equilibrium in favor of the LptB2FG complex
malfunction
Neisseria meningitidis serogroup B / serotype 15
the C-term LptC mutation reduces the stability of the overall LptB2FGC complex, so increased LptB expression compensates by shifting the binding equilibrium in favor of the LptB2FG complex
malfunction
Neisseria meningitidis serogroup B / serotype 15
the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (EC 2.7.8.43), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface
malfunction
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
the C-term LptC mutation reduces the stability of the overall LptB2FGC complex, so increased LptB expression compensates by shifting the binding equilibrium in favor of the LptB2FG complex
-
malfunction
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
the phenotypes of Neisseria meningitidis strains lacking LptB, LptC, LptH (EC 2.7.8.43), LptF, and LptG are identical to those lacking LptD or MsbA, i.e. the knockout mutants are viable but leaky and produce only very little LPS, which is not present at the cell surface
-
physiological function
Neisseria meningitidis serogroup B / serotype 15
biosynthesis of lipopolysaccharide (LPS) in Gram-negative bacteria requires the transport of LPS to its destination, the outer leaflet of the outer membrane. In contrast to Escherichia coli, Neisseria meningitidis can survive without LPS and tolerates inactivation of genes involved in LPS synthesis and transport. LptA, LptB, LptC, LptE, LptF, and LptG proteins are not essential in Neisseria meningitidis and are not required for an essential process such as phospholipid transport. The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis. LptC binds LPS
physiological function
Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the protein-bridge PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. The Lpt subunits form a continuous complex from the inner membrane (IM) to the OM and LPS is propelled along it continuously by the ATPase activity of LptB. Subunit-scale mechanisms of LPS transport include the novel ABC-like mechanism of the LptB2FG subcomplex and the lateral insertion of LPS into the OM by LptD/E, overview. The tightly regulated interactions between these connected subcomplexes suggest a pathway that can react dynamically to membrane stress and may prove to be a valuable target for new antibiotic therapies for Gram-negative pathogens. LPS is synthesized at the cytoplasmic side of the IM before it is transported to the OM. The LptB2FG tetramer extracts LPS from the outer leaflet of the IM and provides the energy to drive LPS transport through an ATPase-dependent mechanism, the LptB2FG complex drives LPS extraction from the IM to the periplasm
physiological function
Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the protein-bridge PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. The Lpt subunits form a continuous complex from the inner membrane (IM) to the OM and LPS is propelled along it continuously by the ATPase activity of LptB. Subunit-scale mechanisms of LPS transport include the novel ABC-like mechanism of the LptB2FG subcomplex and the lateral insertion of LPS into the OM by LptD/E, overview. The tightly regulated interactions between these connected subcomplexes suggest a pathway that can react dynamically to membrane stress and may prove to be a valuable target for new antibiotic therapies for Gram-negative pathogens. LPS is synthesized at the cytoplasmic side of the IM before it is transported to the OM. The LptB2FG tetramer extracts LPS from the outer leaflet of the IM and provides the energy to drive LPS transport through an ATPase-dependent mechanism. the LptB2FG complex drives LPS extraction from the IM to the periplasm
physiological function
Neisseria meningitidis serogroup B / serotype 15
Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the protein-bridge PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. The Lpt subunits form a continuous complex from the inner membrane (IM) to the OM and LPS is propelled along it continuously by the ATPase activity of LptB. Subunit-scale mechanisms of LPS transport include the novel ABC-like mechanism of the LptB2FG subcomplex and the lateral insertion of LPS into the OM by LptD/E, overview. The tightly regulated interactions between these connected subcomplexes suggest a pathway that can react dynamically to membrane stress and may prove to be a valuable target for new antibiotic therapies for Gram-negative pathogens. LPS is synthesized at the cytoplasmic side of the IM before it is transported to the OM. The LptB2FG tetramer extracts LPS from the outer leaflet of the IM and provides the energy to drive LPS transport through an ATPase-dependent mechanism. the LptB2FG complex drives LPS extraction from the IM to the periplasm
physiological function
the enzme is an LPS transporters. LPS transporters are ABC exporters that are known to export extremely hydrophobic compounds, such as lipids, drugs, and steroids. LptB is implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli
physiological function
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the protein-bridge PEZ model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. The Lpt subunits form a continuous complex from the inner membrane (IM) to the OM and LPS is propelled along it continuously by the ATPase activity of LptB. Subunit-scale mechanisms of LPS transport include the novel ABC-like mechanism of the LptB2FG subcomplex and the lateral insertion of LPS into the OM by LptD/E, overview. The tightly regulated interactions between these connected subcomplexes suggest a pathway that can react dynamically to membrane stress and may prove to be a valuable target for new antibiotic therapies for Gram-negative pathogens. LPS is synthesized at the cytoplasmic side of the IM before it is transported to the OM. The LptB2FG tetramer extracts LPS from the outer leaflet of the IM and provides the energy to drive LPS transport through an ATPase-dependent mechanism. the LptB2FG complex drives LPS extraction from the IM to the periplasm
-
physiological function
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
biosynthesis of lipopolysaccharide (LPS) in Gram-negative bacteria requires the transport of LPS to its destination, the outer leaflet of the outer membrane. In contrast to Escherichia coli, Neisseria meningitidis can survive without LPS and tolerates inactivation of genes involved in LPS synthesis and transport. LptA, LptB, LptC, LptE, LptF, and LptG proteins are not essential in Neisseria meningitidis and are not required for an essential process such as phospholipid transport. The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis. LptC binds LPS
-
additional information
identification of the specific subunit-to-subunit interactions that make the continuous transport of LPS from the cytoplasm to the exterior of the outer membrane by Lpt systems possible. The Lpt system is an oligomeric complex consisting of Lpt proteins A through G. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the OM by periplasmic LptA. LptB's catalytic activity couples to the LptF/G heterodimer's extraction of LPS like other ABC transporters, wherein the coupling helices of the TMD interact with the variable Q-loop of the NBD. Structural comparison of ATP-and ADP-bound LptB shows that ATP binding, hydrolysis and release induce conformational changes in the Q-loop region, mediated predominantly by two conserved residues (F90 and R91). LptC may be important to the efficient and stable assembly of the LptB2FG complex, in addition to directly transporting LPS
additional information
identification of the specific subunit-to-subunit interactions that make the continuous transport of LPS from the cytoplasm to the exterior of the outer membrane by Lpt systems possible. The Lpt system is an oligomeric complex consisting of Lpt proteins A through G. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the OM by periplasmic LptA. LptC may be important to the efficient and stable assembly of the LptB2FG complex, in addition to directly transporting LPS
additional information
Neisseria meningitidis serogroup B / serotype 15
identification of the specific subunit-to-subunit interactions that make the continuous transport of LPS from the cytoplasm to the exterior of the outer membrane by Lpt systems possible. The Lpt system is an oligomeric complex consisting of Lpt proteins A through G. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the OM by periplasmic LptA. LptC may be important to the efficient and stable assembly of the LptB2FG complex, in addition to directly transporting LPS
additional information
residue F90 is essential for proper formation of the Lpt inner membrane complex. crystal structures of LptB pre- and post-ATP hydrolysis suggest a role for an active site residue in phosphate exit. Residues E163, H195, and F90 of LptB are required for cell viability. E163 is essential for catalysis, through a bridging water molecule, this glutamate contacts the beta-phosphate of the nucleotide. ATP hydrolysis induces conformational changes. Conformational changes upon ATP hydrolysis show how reorganization of the active site causes changes in the region of LptB believed to interact with LptF/G. The dramatic movement of the switch region observed during ATP hydrolysis plays a critical role in communicating changes in the active site to changes in the transmembrane domains. The groove region of LptB is essential for interaction with inner membrane partners
additional information
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
identification of the specific subunit-to-subunit interactions that make the continuous transport of LPS from the cytoplasm to the exterior of the outer membrane by Lpt systems possible. The Lpt system is an oligomeric complex consisting of Lpt proteins A through G. The membrane-bound LptB, F, G and C subunits are connected to the LptD/E heterodimer in the OM by periplasmic LptA. LptC may be important to the efficient and stable assembly of the LptB2FG complex, in addition to directly transporting LPS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E163Q
site-directed mutagenesis, catalytically inactive variant, introduction of plasmid-encoded LptBE163Q-His8 variant into the wild-type strain results in increased outer membrane permeability, dominant-negative phenotype
F90A
site-directed mutagenesis, catalytically inactive variant, the F90A variant cannot form a stable complex with the Lpt-inner membrane components
F90Y
site-directed mutagenesis, the LptB and LptB-His8 F90Y variants are functional in vivo
H195A
site-directed mutagenesis, catalytically inactive variant, introduction of plasmid-encoded LptB-H195A-His8 variant into the wild-type strain results in increased outer membrane permeability, dominant-negative phenotype
additional information
amorphadiene, the precursor of antimalarial drug artemisinin from Artemisia annua, is secreted from Escherichia coli cells overexpressing the biosynthetic pathway. The overexpression of transporters in the lipopolysaccharide transport system (msbA, lptD, lptCABFG) improves amorphadiene (AD) production. AD production in both early stage (8 h) and final stage (24 h) is increased by more than twofold in the strains that overexpress lptCABFG or msbA. But co-overexpression of LptCABFG and LptD or LptD and TolC does not enhance AD-specific production synergistically, despite the fact that the AD titer is increased mainly due to the increased cell density, overview
additional information
construction of chromosomal deletion of lptB and replacement with a kanamycin-resistance cassette (DELTAlptB:: kan allele), where the region from the second codon to the stop codon of lptB is deleted
additional information
Neisseria meningitidis serogroup B / serotype 15
construction of a several HB-1DELTAlptB lptB deletion mutants, phenotypes, overview. The expression of PagL in the lptH, lptC, lptF, and lptG mutants does not affect LPS mobility, demonstrating that the residual LPS present in these strains does not reach the cell surface. PagL is an outer membrane (OM) enzyme that can remove an acyl chain from LPS when LPS is present at its proper location, i.e. the outer leaflet of the OM
additional information
Neisseria meningitidis serogroup B / serotype 15 H44/76
-
construction of a several HB-1DELTAlptB lptB deletion mutants, phenotypes, overview. The expression of PagL in the lptH, lptC, lptF, and lptG mutants does not affect LPS mobility, demonstrating that the residual LPS present in these strains does not reach the cell surface. PagL is an outer membrane (OM) enzyme that can remove an acyl chain from LPS when LPS is present at its proper location, i.e. the outer leaflet of the OM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Suits, M.D.; Sperandeo, P.; Deho, G.; Polissi, A.; Jia, Z.
Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis
J. Mol. Biol.
380
476-488
2008
Escherichia coli
brenda
Ward, A.B.; Guvench, O.; Hills, R.D.
Coarse grain lipid-protein molecular interactions and diffusion with MsbA flippase
Proteins
80
2178-2190
2012
Vibrio cholerae (Q9KQW9)
brenda
Zhang, C.; Chen, X.; Stephanopoulos, G.; Too, H.P.
Efflux transporter engineering markedly improves amorphadiene production in Escherichia coli
Biotechnol. Bioeng.
113
1755-1763
2016
Escherichia coli (P0A9V1)
brenda
Hicks, G.; Jia, Z.
Structural basis for the lipopolysaccharide export activity of the bacterial lipopolysaccharide transport system
Int. J. Mol. Sci.
19
E2680
2018
Escherichia coli (P0A9V1), Neisseria meningitidis serogroup B / serotype 15 (E6MYT4), Neisseria meningitidis serogroup B / serotype 15 H44/76 (E6MYT4), Pseudomonas aeruginosa (A0A071L2Z5)
brenda
Bos, M.P.; Tommassen, J.
The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis
J. Biol. Chem.
286
28688-28696
2011
Neisseria meningitidis serogroup B / serotype 15 (E6MYT4), Neisseria meningitidis serogroup B / serotype 15 H44/76 (E6MYT4)
brenda
Sherman, D.J.; Lazarus, M.B.; Murphy, L.; Liu, C.; Walker, S.; Ruiz, N.; Kahne, D.
Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport
Proc. Natl. Acad. Sci. USA
111
4982-4987
2014
Escherichia coli (P0A9V1)
brenda