2ch4
From Proteopedia
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==Overview== | ==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 .. | + | 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 the CheW receptor clamps for binding receptor tips., Linking layers of ternary complexes with close-packed receptors generates, a lattice with reasonable component ratios, cooperative interactions among, receptors and accessible sites for modification enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 2CH4 is a | + | 2CH4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ANP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CH4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:42:49 2007'' |
Revision as of 12:37, 5 November 2007
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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 the CheW receptor clamps for binding receptor tips., Linking layers of ternary complexes with close-packed receptors generates, a lattice with reasonable component ratios, cooperative interactions among, receptors and accessible sites for modification enzymes.
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
Page seeded by OCA on Mon Nov 5 14:42:49 2007
