3JZ3

Structure of the cytoplasmic segment of histidine kinase QseC

Summary for 3JZ3

• Entry DOI: 10.2210/pdb3jz3/pdb
• Descriptor: Sensor protein qseC, SULFATE ION (3 entities in total)
• Functional Keywords: helix-turn-helix, kinase domain, atp-binding, cell inner membrane, cell membrane, kinase, membrane, nucleotide-binding, phosphoprotein, transferase, transmembrane, two-component regulatory system, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P40719
• Total number of polymer chains: 2
• Total formula weight: 49561.22

Authors

Xie, W.,Kwiatkowski, W.,Choe, S.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2009-09-22, release date: 2010-07-21, Last modification date: 2012-04-04)

Primary citation

Xie, W.,Dickson, C.,Kwiatkowski, W.,Choe, S.
Structure of the Cytoplasmic Segment of Histidine Kinase Receptor QseC, a Key Player in Bacterial Virulence.
Protein Pept.Lett., 17:1383-1391, 2010

PubMed 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 QseC-CD provides a platform for developing more potent inhibitors of pathogen virulence.

PubMed: 20594156

Experimental method

X-RAY DIFFRACTION (2.5 Å)