3jz3

Structure of the cytoplasmic segment of histidine kinase QseC

spinqualitylabelsall models 3jz3, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jz3 is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Gene: qseC, ygiY, b3026, JW2994 (ECOLI) Activity: Histidine kinase, with EC number 2.7.13.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [QSEC_ECOLI] Member of a two-component regulatory system QseB/QseC. Activates the flagella regulon by activating transcription of FlhDC. May activate QseB by phosphorylation. 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 QseC is a histidine kinase (HK) receptor involved in quorum sensing, a mechanism by which bacteria respond to fluctuations in cell population. We conducted a structural study of the cytoplasmic domain of QseC (QseC-CD) using X-ray crystallography. The 2.5 A structure of the apo-enzyme revealed that the kinase domain of QseC retains the overall fold of the typical HK kinase domain. The construct that we used is inactive in the autokinase reaction and its inactivity is most likely caused by its atypical dimerization interface, as compared to that observed in the T.maritima HK cytoplasmic domain structure. Restoration of the activity may require that the entire dimerization domain be present in the protein construct. QseC, which plays an important role in bacterial pathogenesis, is a promising drug target and the structure of QseC-CD provides a platform for developing more potent inhibitors of pathogen virulence. Structure of the Cytoplasmic Segment of Histidine Kinase Receptor QseC, a Key Player in Bacterial Virulence.,Xie W, Dickson C, Kwiatkowski W, Choe S Protein Pept Lett. 2010 Jul 1. PMID:20594156 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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