BRENDA - Enzyme Database show
show all sequences of 2.7.8.43

EptC of Campylobacter jejuni mediates phenotypes involved in host interactions and virulence

Cullen, T.W.; O'Brien, O.P.; Hendrixson, D.R.; Giles, D.K.; Hobb, R.I.; Thompson, S.A.; Brodbelt, J.S.; Trent, M.S.; Infect. Immun. 81, 430-4440 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene cj0256 or eptC
Campylobacter jejuni
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of several enzyme mutant strains, overview
Campylobacter jejuni
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni
-
?
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni 81-176
-
?
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
additional information
Campylobacter jejuni
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
?
-
-
-
additional information
Campylobacter jejuni 81-176
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Campylobacter jejuni
A0A0E1EWJ6
gene cj0256 or eptC
-
Campylobacter jejuni 81-176
A0A0E1EWJ6
gene cj0256 or eptC
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
733966
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
733966
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni 81-176
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
733966
Campylobacter jejuni
?
-
-
-
-
additional information
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
733966
Campylobacter jejuni 81-176
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
gene cj0256 or eptC
Campylobacter jejuni
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of several enzyme mutant strains, overview
Campylobacter jejuni
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni
-
?
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
Campylobacter jejuni 81-176
-
?
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
?
diacylphosphatidylethanolamine + lipid A
Campylobacter jejuni 81-176
-
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
?
additional information
Campylobacter jejuni
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
?
-
-
-
additional information
Campylobacter jejuni 81-176
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
733966
Campylobacter jejuni
?
-
-
-
?
diacylphosphatidylethanolamine + flagellar rod protein FlgG
-
733966
Campylobacter jejuni 81-176
?
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni 81-176
diacylglycerol + lipid A 1-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
diacylphosphatidylethanolamine + lipid A
-
733966
Campylobacter jejuni 81-176
diacylglycerol + lipid A 4'-(2-aminoethyl diphosphate)
-
-
-
?
additional information
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
733966
Campylobacter jejuni
?
-
-
-
-
additional information
enzyme EptC catalyzes the addition of phosphoethanolamine to the first heptose sugar (Hep I) of the inner core oligosaccharide of Campylobacter jejuni lipooligosaccharide
733966
Campylobacter jejuni 81-176
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
strains lacking gene eptC show decreased commensal colonization of chick ceca and reduced colonization of BALB/cByJ mice compared to wild-type strains
Campylobacter jejuni
physiological function
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue. The enzyme also catalyzes the addition of phosphoethanolamine to the first heptose sugar of the inner core oligosaccharide of lipooligosaccharide, a fourth enzymatic target. Modification of Campylobacter jejuni lipid A with phosphoethanolamine results in increased recognition by the human Toll-like receptor 4-myeloid differentiation factor 2 complex, along with providing resistance to relevant mammalian and avian antimicrobial peptides (i.e., defensins). Modification of surface structures with phosphoethanolamine by EptC is key to its ability to promote commensalism in an avian host and to survive in the mammalian gastrointestinal environment. Modification of FlgG is required for efficient flagellar production and motility
Campylobacter jejuni
General Information (protein specific)
General Information
Commentary
Organism
malfunction
strains lacking gene eptC show decreased commensal colonization of chick ceca and reduced colonization of BALB/cByJ mice compared to wild-type strains
Campylobacter jejuni
physiological function
the enzyme EptC serves a dual role in modifying the flagellar rod protein, FlgG, and the lipid A domain lipooligosaccharide with a pEtN residue. The enzyme also catalyzes the addition of phosphoethanolamine to the first heptose sugar of the inner core oligosaccharide of lipooligosaccharide, a fourth enzymatic target. Modification of Campylobacter jejuni lipid A with phosphoethanolamine results in increased recognition by the human Toll-like receptor 4-myeloid differentiation factor 2 complex, along with providing resistance to relevant mammalian and avian antimicrobial peptides (i.e., defensins). Modification of surface structures with phosphoethanolamine by EptC is key to its ability to promote commensalism in an avian host and to survive in the mammalian gastrointestinal environment. Modification of FlgG is required for efficient flagellar production and motility
Campylobacter jejuni
Other publictions for EC 2.7.8.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750867
Hicks
-
Structural basis for the lipo ...
Escherichia coli
Int. J. Mol. Sci.
19
E2680
2018
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1
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1
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1
1
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752134
Schultz
Lipopolysaccharide binding to ...
Escherichia coli
Protein Sci.
26
1517-1523
2017
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1
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14
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1
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1
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14
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1
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1
1
1
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3
3
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738476
Liu
A phosphoethanolamine transfer ...
Cronobacter sakazakii, Cronobacter sakazakii BAA894
J. Appl. Microbiol.
121
1444-1456
2016
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1
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1
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2
2
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733635
Handing
The lipooligosaccharide-modify ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Cell. Microbiol.
17
910-921
2015
-
-
1
-
1
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2
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4
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2
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2
2
-
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735018
Trombley
Phosphoethanolamine transferas ...
Haemophilus ducreyi, Haemophilus ducreyi ATCC 700724
PLoS ONE
10
e0124373
2015
-
-
1
-
1
-
-
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1
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7
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5
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5
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2
3
-
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-
739106
Nowicki
Extracellular zinc induces pho ...
Pseudomonas aeruginosa
Mol. Microbiol.
97
166-178
2015
-
-
1
-
1
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1
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1
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4
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1
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2
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1
2
2
1
-
-
740532
Telke
Functional genomics to discove ...
Shewanella algae, Shewanella algae MARS 14
Int. J. Antimicrob. Agents
46
648-652
2015
-
-
1
-
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2
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2
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4
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1
1
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738368
Packiam
Phosphoethanolamine decoration ...
Neisseria gonorrhoeae, Neisseria gonorrhoeae FA 1090
Infect. Immun.
82
2170-2179
2014
-
-
-
-
1
-
-
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2
-
11
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2
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2
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2
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-
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2
2
-
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739495
Piek
The role of oxidoreductases in ...
Neisseria meningitidis, Neisseria meningitidis NMB
PLoS ONE
9
e106513
2014
1
-
1
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1
1
1
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1
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1
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8
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1
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1
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1
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739786
Fage
Crystallographic study of the ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Acta Crystallogr. Sect. D
70
2730-2739
2014
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1
1
6
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1
1
1
7
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3
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1
1
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12
2
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1
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1
6
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7
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1
1
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12
2
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3
3
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752031
Sherman
Decoupling catalytic activity ...
Neisseria meningitidis serogroup B, Neisseria meningitidis serogroup B MC58
Proc. Natl. Acad. Sci. USA
111
4982-4987
2014
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2
2
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733965
Lewis
Phosphoethanolamine residues o ...
Neisseria gonorrhoeae
Infect. Immun.
81
33-42
2013
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2
2
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733966
Cullen
EptC of Campylobacter jejuni m ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Infect. Immun.
81
430-4440
2013
-
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1
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1
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8
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3
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8
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8
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2
2
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734476
Wanty
The structure of the neisseria ...
Neisseria meningitidis, Neisseria meningitidis NMB
J. Mol. Biol.
425
3389-3402
2013
-
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1
1
1
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1
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3
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6
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8
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1
1
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12
1
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2
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1
1
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1
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6
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1
1
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12
1
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3
4
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740134
Bontemps-Gallo
Biosynthesis of osmoregulated ...
Escherichia coli
BioMed Res. Int.
2013
371429
2013
1
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1
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1
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1
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1
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3
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1
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2
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1
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1
1
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740516
Knirel
O-antigen structure of Shigell ...
Shigella flexneri
Glycobiology
23
475-485
2013
-
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1
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3
-
4
-
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3
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5
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1
1
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733017
Anandan
Cloning, expression, purificat ...
Neisseria meningitidis, Neisseria meningitidis NMB
Acta Crystallogr. Sect. F
68
1494-1497
2012
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