analysis of the cobinamide (Cbi)-bound BtuF crystal structure model, PDB ID 5M29, crystal structures of Cbi-bound BtuF mutants W66F, W66Y and W66L, sitting drop vapor diffusion technique, mixing of 20 mg/ml protein in 10 mM Tris pH 8 and 100 mM NaCl, with precipitant solution containing 1% w/v tryptone, 50 mM HEPES, pH 7.0, and 12% w/v PEG 3350, 1-2 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution, molecular replacement using the BtuF structure (PDB ID 1N2Z) as search model
Escherichia coli
additional information
site-directed mutagenesis of tryptophan residue W66 in the substrate binding cleft , the affinity for cobinamide of the W66X mutants is lower except for W66F. Three mutants with impaired Cbi binding (W66A, W66R, and W66E) and one with high binding affinity (W66F) are used for transport assays. Despite having lower Cbi binding affinities, Cbi transport is hardly affected by W66X substitution
Escherichia coli
W66A
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66E
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66F
site-directed mutagenesis, does not reduce the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66H
site-directed mutagenesis, reduces the affinity for cobinamide 10fold compared to wild-type
Escherichia coli
W66L
site-directed mutagenesis, reduces the affinity for cobinamide 3fold compared to wild-type
Escherichia coli
W66R
site-directed mutagenesis, reduces the affinity for cobinamide 10fold compared to wild-type
Escherichia coli
W66Y
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
ATP + H2O + cobinamide-[cobalamin-binding protein][side 1]
752221
Escherichia coli
ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1]
?
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
752221
Escherichia coli
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
?
additional information
BtuCD-F catalyzes the uptake of cobinamide, a cobalamin precursor, and cobalamin. BtuCD-catalyzed in vitro transport of cyano-cobinamide and of cobalamin is ATP- and BtuF-dependent. Tryptophan residue W66 of BtuF is involved in the substrate binding of cobalamin
752221
Escherichia coli
?
analysis of the cobinamide (Cbi)-bound BtuF crystal structure model, PDB ID 5M29, crystal structures of Cbi-bound BtuF mutants W66F, W66Y and W66L, sitting drop vapor diffusion technique, mixing of 20 mg/ml protein in 10 mM Tris pH 8 and 100 mM NaCl, with precipitant solution containing 1% w/v tryptone, 50 mM HEPES, pH 7.0, and 12% w/v PEG 3350, 1-2 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution, molecular replacement using the BtuF structure (PDB ID 1N2Z) as search model
Escherichia coli
additional information
site-directed mutagenesis of tryptophan residue W66 in the substrate binding cleft , the affinity for cobinamide of the W66X mutants is lower except for W66F. Three mutants with impaired Cbi binding (W66A, W66R, and W66E) and one with high binding affinity (W66F) are used for transport assays. Despite having lower Cbi binding affinities, Cbi transport is hardly affected by W66X substitution
Escherichia coli
W66A
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66E
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66F
site-directed mutagenesis, does not reduce the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
W66H
site-directed mutagenesis, reduces the affinity for cobinamide 10fold compared to wild-type
Escherichia coli
W66L
site-directed mutagenesis, reduces the affinity for cobinamide 3fold compared to wild-type
Escherichia coli
W66R
site-directed mutagenesis, reduces the affinity for cobinamide 10fold compared to wild-type
Escherichia coli
W66Y
site-directed mutagenesis, reduces the affinity for cobinamide severalfold compared to wild-type
Escherichia coli
ATP + H2O + cobinamide-[cobalamin-binding protein][side 1]
752221
Escherichia coli
ADP + phosphate + cobinamide[side 2] + [cobalamin-binding protein][side 1]
?
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
752221
Escherichia coli
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
?
additional information
BtuCD-F catalyzes the uptake of cobinamide, a cobalamin precursor, and cobalamin. BtuCD-catalyzed in vitro transport of cyano-cobinamide and of cobalamin is ATP- and BtuF-dependent. Tryptophan residue W66 of BtuF is involved in the substrate binding of cobalamin
752221
Escherichia coli
?
malfunction
substitution of W66 in BtuF with tyrosine or leucine reduced the affinity 3fold compared to wild-type, and a change to histidine or arginine reduces it more than 10fold
Escherichia coli
additional information
the crystal structure of cobinamide-bound BtuF reveals a conformational change of a tryptophan residue W66 in the substrate binding cleft compared to the structure of cobalamin-bound BtuF, molecular dynamics simulations. BtuF is a class III periplasmic substrate binding protein
Escherichia coli
physiological function
ATP-binding cassette (ABC) transporters are a large family of integral membrane proteins and involved in nutrient uptake, drug extrusion, and lipid homeostasis. They use the energy of ATP binding and hydrolysis to power substrate transport across the lipid bilayer. BtuCD-F is an ABC transporter that mediates cobalamin (Cbl) uptake into Escherichia coli, Escherichia coli is unable to synthesize Cbl de novo. BtuCD-F might also be involved in the uptake of cobinamide, a cobalamin precursor. Precursor cobinamide (Cbi) lacks the 5,6-dimethylbenzimidazole (DMB) moiety and sugar-phosphate linker and is therefore smaller than Cbl. BtuCD-catalyzed in vitro transport of cyano-cobinamide is ATP- and BtuF-dependent. BtuF residue W66 is important for high affinity Cbi binding, but not for substrate delivery or transport
Escherichia coli
malfunction
substitution of W66 in BtuF with tyrosine or leucine reduced the affinity 3fold compared to wild-type, and a change to histidine or arginine reduces it more than 10fold
Escherichia coli
additional information
the crystal structure of cobinamide-bound BtuF reveals a conformational change of a tryptophan residue W66 in the substrate binding cleft compared to the structure of cobalamin-bound BtuF, molecular dynamics simulations. BtuF is a class III periplasmic substrate binding protein
Escherichia coli
physiological function
ATP-binding cassette (ABC) transporters are a large family of integral membrane proteins and involved in nutrient uptake, drug extrusion, and lipid homeostasis. They use the energy of ATP binding and hydrolysis to power substrate transport across the lipid bilayer. BtuCD-F is an ABC transporter that mediates cobalamin (Cbl) uptake into Escherichia coli, Escherichia coli is unable to synthesize Cbl de novo. BtuCD-F might also be involved in the uptake of cobinamide, a cobalamin precursor. Precursor cobinamide (Cbi) lacks the 5,6-dimethylbenzimidazole (DMB) moiety and sugar-phosphate linker and is therefore smaller than Cbl. BtuCD-catalyzed in vitro transport of cyano-cobinamide is ATP- and BtuF-dependent. BtuF residue W66 is important for high affinity Cbi binding, but not for substrate delivery or transport
Escherichia coli
749978
Agarwal
Mechanistic basis of vitamin ...
Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 ATCC 39541, Vibrio cholerae serotype O1 Classical Ogawa 395, Vibrio cholerae serotype O1 O395
Biochim. Biophys. Acta
1867
140-151
2019
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1
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749821
Okamoto
Characterization of human ATP ...
Homo sapiens
Biochem. Biophys. Res. Commun.
496
1122-1127
2018
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2
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1
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1
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2
2
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750412
Santos
Functional and structural cha ...
Lactobacillus delbrueckii subsp. bulgaricus, Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842, Lactobacillus delbrueckii subsp. bulgaricus DSM 20081, Lactobacillus delbrueckii subsp. bulgaricus JCM 1002, Lactobacillus delbrueckii subsp. bulgaricus NBRC 13953, Lactobacillus delbrueckii subsp. bulgaricus NCIMB 11778
eLife
7
e35828
2018
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1
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12
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18
1
1
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1
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2
2
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751644
Schmitt
Vitamin B12 import is all abo ...
Escherichia coli
Nat. Chem. Biol.
14
640-641
2018
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1
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1
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2
2
-
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751670
Rempel
Cysteine-mediated decyanation ...
Thiobacillus denitrificans
Nat. Commun.
9
3038
2018
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1
1
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1
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3
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751661
Goudsmits
Single-molecule visualization ...
Escherichia coli
Nat. Commun.
8
1652
2017
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1
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5
1
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752215
Mireku
Structural basis of nanobody- ...
Escherichia coli
Sci. Rep.
7
14296
2017
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752221
Mireku
Conformational change of a tr ...
Escherichia coli
Sci. Rep.
7
41575
2017
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1
1
8
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8
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3
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1
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3
3
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750063
Priess
Release of entropic spring re ...
Escherichia coli
Biophys. J.
110
2407-2418
2016
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1
1
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1
1
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1
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2
2
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751956
Pan
ATP hydrolysis induced confor ...
Escherichia coli
PLoS ONE
11
e0166980
2016
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2
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2
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752200
Kawaguchi
Translocation of the ABC tran ...
Homo sapiens
Sci. Rep.
6
30183
2016
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1
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1
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3
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2
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734003
Su
Conformational motions and fun ...
Escherichia coli
Int. J. Mol. Sci.
16
17933-17951
2015
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734281
Joseph
Conformational cycle of the vi ...
Escherichia coli
J. Biol. Chem.
289
3176-3185
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734760
Korkhov
Structure of AMP-PNP-bound Btu ...
Escherichia coli
Nat. Struct. Mol. Biol.
21
1097-1099
2014
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734820
Gopinath
A vitamin B12 transporter in M ...
Mycobacterium tuberculosis
Open Biology
3
120175
2013
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Korkhov
Asymmetric states of vitamin B ...
Escherichia coli
FEBS Lett.
586
972-976
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Weng
-
The conformational transition ...
Escherichia coli
PLoS ONE
7
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734771
Korkhov
Structure of AMP-PNP-bound vit ...
Escherichia coli
Nature
490
367-372
2012
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Di Bartolo
In vitro folding and assembly ...
Escherichia coli
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286
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Joseph
Transmembrane gate movements i ...
Escherichia coli
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286
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2011
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Lewinson
A distinct mechanism for the A ...
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713485
Kandt
Holo-BtuF stabilizes the open ...
Escherichia coli
Proteins
78
738-753
2010
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Sun
Molecular dynamics simulation ...
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620-630
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