2v25

From Proteopedia

Revision as of 15:37, 30 October 2007

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. ... [(full description)]

About this Structure

2V25 is a [Single protein] structure of sequence from [Campylobacter jejuni] with ZN and ASP as [ligands]. Structure known Active Site: AC1. 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 MD, Dodson E, Wilson KS, Wilkinson AJ, Kelly DJ, J Mol Biol. 2007 Jun 19;. PMID:17631313

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