This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2v25

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v25.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2v25.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v25| PDB=2v25 | SCENE= }}
{{STRUCTURE_2v25| PDB=2v25 | SCENE= }}
-
'''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===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17631313}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17631313 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17631313}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Transport]]
[[Category: Transport]]
[[Category: Virulence factor]]
[[Category: Virulence factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:04:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:39:59 2008''

Revision as of 02:40, 29 July 2008

Image:2v25.png

Template:STRUCTURE 2v25

STRUCTURE OF THE CAMPYLOBACTER JEJUNI ANTIGEN PEB1A, AN ASPARTATE AND GLUTAMATE RECEPTOR WITH BOUND ASPARTATE

Template:ABSTRACT PUBMED 17631313

About this Structure

2V25 is a Single protein structure of sequence from Campylobacter jejuni. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Tue Jul 29 05:39:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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