2qdl

Crystal structure of scaffolding protein TtCheW from Thermoanaerobacter tengcongensis

spinqualitylabelsall models 2qdl, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qdl is a 2 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis MB4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RBV8_CALS4 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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