2ch4

From Proteopedia

Revision as of 15:03, 30 October 2007

COMPLEX BETWEEN BACTERIAL CHEMOTAXIS HISTIDINE KINASE CHEA DOMAINS P4 AND P5 AND RECEPTOR-ADAPTOR PROTEIN CHEW

Overview

In bacterial chemotaxis, an assembly of transmembrane receptors, the CheA, histidine kinase and the adaptor protein CheW processes environmental, stimuli to regulate motility. The structure of a Thermotoga maritima, receptor cytoplasmic domain defines CheA interaction regions and metal, ion-coordinating charge centers that undergo chemical modification to tune, receptor response. Dimeric CheA-CheW, defined by crystallography and, pulsed ESR, positions two CheWs to form a cleft that is lined with, residues important for receptor interactions and sized to clamp one, receptor dimer. CheW residues involved in kinase activation map to, interfaces that orient the CheW clamps. CheA regulatory domains associate, in crystals through conserved hydrophobic surfaces. Such CheA, self-contacts align ... [(full description)]

About this Structure

2CH4 is a [Protein complex] structure of sequences from [Thermotoga maritima] with ANP as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Reconstruction of the chemotaxis receptor-kinase assembly., Park SY, Borbat PP, Gonzalez-Bonet G, Bhatnagar J, Pollard AM, Freed JH, Bilwes AM, Crane BR, Nat Struct Mol Biol. 2006 May;13(5):400-7. Epub 2006 Apr 23. PMID:16622408

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