2qdl

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qdl OCA], [http://www.ebi.ac.uk/pdbsum/2qdl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qdl RCSB]</span>
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[[Category: Shi, L.]]
[[Category: Shi, L.]]
[[Category: Yao, W.]]
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[[Category: GOL]]
 
[[Category: beta-barrel]]
[[Category: beta-barrel]]
[[Category: signaling protein]]
[[Category: signaling protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:48:00 2008''

Revision as of 01:48, 31 March 2008


PDB ID 2qdl

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of scaffolding protein TtCheW from Thermoanaerobacter tengcongensis


Overview

The crystal structure of the scaffolding protein CheW from Thermoanaerobacter tengcongensis (TtCheW) is reported with a resolution at 2.2A using molecular replacement. Based on the crystal structure TmCheA P4-P5-TmCheW from Thermotoga maritime reported by others, we modeled the TmCheA P4-P5-TtCheW complex and predicted that TtCheW is involved in a hydrophobic interaction with CheA, similar to that for TmCheW. We also found that the conserved motif "NxxGxIxP" from CheW plays an important role in CheA binding. The coincidence of the reported mutation sites related to CheW-MCP binding, and the predicted protein interaction region within the TtCheW molecule, suggest that CheW-MCP binding sites lie in the groove-shaped area between TtCheW and the CheA P4 domain within the assembled model.

About this Structure

2QDL is a Single protein structure of sequence from Thermoanaerobacter tengcongensis. Full crystallographic information is available from OCA.

Reference

Crystal structure of scaffolding protein CheW from thermoanaerobacter tengcongensis., Yao W, Shi L, Liang DC, Biochem Biophys Res Commun. 2007 Oct 5;361(4):1027-32. Epub 2007 Jul 31. PMID:17681283

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