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2v25

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Revision as of 08:34, 12 September 2018

Structure of the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate

Structural highlights

2v25 is a 2 chain structure with sequence from "campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PEB1A_CAMJE] Common antigen and a major cell adherence molecule. Most probably involved, with PEB1C, in a binding-protein-dependent transport system for an amino acid. May be involved in binding to intestinal cells.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The PEB1a protein is an antigenic factor exposed on the surface of the food-borne human pathogen Campylobacter jejuni, which has a major role in adherence and host colonisation. PEB1a is also the periplasmic binding protein component of an aspartate/glutamate ABC transporter essential for optimal microaerobic growth on these dicarboxylic amino acids. Here, we report the crystal structure of PEB1a at 1.5 A resolution. The protein has a typical two-domain alpha/beta structure, characteristic of periplasmic extracytoplasmic solute receptors and a chain topology related to the type II subfamily. An aspartate ligand, clearly defined by electron density in the interdomain cleft, forms extensive polar interactions with the protein, the majority of which are made with the larger domain. Arg89 and Asp174 form ion-pairing interactions with the main chain alpha-carboxyl and alpha-amino-groups, respectively, of the ligand, while Arg67, Thr82, Lys19 and Tyr156 co-ordinate the ligand side-chain carboxyl group. Lys19 and Arg67 line a positively charged groove, which favours binding of Asp over the neutral Asn. The ligand-binding cleft is of sufficient depth to accommodate a glutamate. This is the first structure of an ABC-type aspartate-binding protein, and explains the high affinity of the protein for aspartate and glutamate, and its much weaker binding of asparagine and glutamine. Stopped-flow fluorescence spectroscopy indicates a simple bimolecular mechanism of ligand binding, with high association rate constants. Sequence alignments and phylogenetic analyses revealed PEB1a homologues in some Gram-positive bacteria. The alignments suggest a more distant homology with GltI from Escherichia coli, a known glutamate and aspartate-binding protein, but Lys19 and Tyr156 are not conserved in GltI. Our results provide a structural basis for understanding both the solute transport and adhesin/virulence functions of PEB1a.

A bacterial virulence factor with a dual role as an adhesin and a solute-binding protein: the crystal structure at 1.5 A resolution of the PEB1a protein from the food-borne human pathogen Campylobacter jejuni.,Muller A, Leon-Kempis Mdel R, Dodson E, Wilson KS, Wilkinson AJ, Kelly DJ J Mol Biol. 2007 Sep 7;372(1):160-71. Epub 2007 Jun 19. PMID:17631313^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Muller A, Leon-Kempis Mdel R, Dodson E, Wilson KS, Wilkinson AJ, Kelly DJ. A bacterial virulence factor with a dual role as an adhesin and a solute-binding protein: the crystal structure at 1.5 A resolution of the PEB1a protein from the food-borne human pathogen Campylobacter jejuni. J Mol Biol. 2007 Sep 7;372(1):160-71. Epub 2007 Jun 19. PMID:17631313 doi:http://dx.doi.org/10.1016/j.jmb.2007.06.041

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v25"

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-==STRUCTURE OF THE CAMPYLOBACTER JEJUNI ANTIGEN PEB1A, AN ASPARTATE AND GLUTAMATE RECEPTOR WITH BOUND ASPARTATE==
+==Structure of the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate==
 <StructureSection load='2v25' size='340' side='right' caption='[[2v25]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
@@ Line 13: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/2v25_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v2/2v25_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 35: / Line 35: @@
 [[Category: Dodson, E]]
 [[Category: Kelly, D J]]
-[[Category: Leon-Kempis, M Del Rocio]]
+[[Category: Leon-Kempis, M del Rocio]]
 [[Category: Muller, A]]
 [[Category: Wilkinson, A J]]

2v25

From Proteopedia

Revision as of 08:34, 12 September 2018

Structure of the Campylobacter jejuni antigen Peb1A, an aspartate and glutamate receptor with bound aspartate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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