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PDBsum entry 3jz3
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References listed in PDB file
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Key reference
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Title
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Structure of the cytoplasmic segment of histidine kinase receptor qsec, A key player in bacterial virulence.
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Authors
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W.Xie,
C.Dickson,
W.Kwiatkowski,
S.Choe.
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Ref.
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Protein Pept Lett, 2010,
17,
1383-1391.
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PubMed id
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Abstract
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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 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.
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