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Structure of the Cytoplasmic Segment of Histidine Kinase Receptor QseC: A Key Player in Bacterial Virulence

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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 Å 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 QseCCD provides a platform for developing more potent inhibitors of pathogen virulence.

Keywords: (CA); (DHp); (EPI/NEI); (HK); (NCS); (RR); (TM1); (TM2); ATP; Crystal Packi; Cytoplasmic domain; DLS; DMPC; E.coli E22; Gel-electrophoresis; HAMP; HK/RRs; HK853-CD); Nucleotide; PISA server; PyMOL; S.typhimurium; T.maritima; Virulence†; X-ray crystallography; domain; flhDC; histidine; histidine kinase; melittin; phosphorylation; quorum; quorum sensing; response; response regulator; systems; two-component; two-component regulatory systems

Document Type: Research Article

Publication date: November 1, 2010

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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