2qdl
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(New page: 200px<br /><applet load="2qdl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qdl, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 11:46, 23 January 2008
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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 with as ligand. 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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