Abstract
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: Cytoplasmic domain, histidine kinase, phosphorylation, quorum sensing, response regulator, two-component regulatory systems, domain, histidine, quorum, response, two-component, systems, Virulence†, (HK), X-ray crystallography, T.maritima, (RR), (TM1), (TM2), (DHp), (CA), ATP, HAMP, HK/RRs, (EPI/NEI), flhDC, E.coli E22, HK853-CD), (NCS), PyMOL, melittin, DMPC, DLS, Gel-electrophoresis, Nucleotide, Crystal Packi, PISA server, S.typhimurium
Protein & Peptide Letters
Title: Structure of the Cytoplasmic Segment of Histidine Kinase Receptor QseC: A Key Player in Bacterial Virulence
Volume: 17 Issue: 11
Author(s): Wei Xie, Chris Dickson, Witek Kwiatkowski and Senyon Choe
Affiliation:
Keywords: Cytoplasmic domain, histidine kinase, phosphorylation, quorum sensing, response regulator, two-component regulatory systems, domain, histidine, quorum, response, two-component, systems, Virulence†, (HK), X-ray crystallography, T.maritima, (RR), (TM1), (TM2), (DHp), (CA), ATP, HAMP, HK/RRs, (EPI/NEI), flhDC, E.coli E22, HK853-CD), (NCS), PyMOL, melittin, DMPC, DLS, Gel-electrophoresis, Nucleotide, Crystal Packi, PISA server, S.typhimurium
Abstract: 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.
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Cite this article as:
Xie Wei, Dickson Chris, Kwiatkowski Witek and Choe Senyon, Structure of the Cytoplasmic Segment of Histidine Kinase Receptor QseC: A Key Player in Bacterial Virulence, Protein & Peptide Letters 2010; 17 (11) . https://dx.doi.org/10.2174/0929866511009011383
DOI https://dx.doi.org/10.2174/0929866511009011383 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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