2QDL

Crystal structure of scaffolding protein TtCheW from Thermoanaerobacter tengcongensis

Summary for 2QDL

• Entry DOI: 10.2210/pdb2qdl/pdb
• Descriptor: Chemotaxis signal transduction protein, GLYCEROL (3 entities in total)
• Functional Keywords: beta-barrel, signaling protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 2
• Total formula weight: 37385.77

Authors

Yao, W.,Shi, L.,Liang, D.C. (deposition date: 2007-06-21, release date: 2007-09-04, Last modification date: 2023-08-30)

Primary citation

Yao, W.,Shi, L.,Liang, D.C.
Crystal structure of scaffolding protein CheW from thermoanaerobacter tengcongensis.
Biochem.Biophys.Res.Commun., 361:1027-1032, 2007

PubMed Abstract: 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.

PubMed: 17681283
DOI: 10.1016/j.bbrc.2007.07.130

Experimental method

X-RAY DIFFRACTION (2.2 Å)