2qdl
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | The crystal structure of the scaffolding protein CheW from | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoanaerobacter tengcongensis]] | [[Category: Thermoanaerobacter tengcongensis]] | ||
| - | [[Category: Liang, D | + | [[Category: Liang, D C.]] |
[[Category: Shi, L.]] | [[Category: Shi, L.]] | ||
[[Category: Yao, W.]] | [[Category: Yao, W.]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:26 2008'' |
Revision as of 16:38, 21 February 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
Page seeded by OCA on Thu Feb 21 18:38:26 2008
