3mpl

Crystal Structure of Bordetella pertussis BvgS VFT2 domain (Double Mutant F375E/Q461E)Crystal Structure of Bordetella pertussis BvgS VFT2 domain (Double Mutant F375E/Q461E)

Structural highlights 3mpl is a 1 chain structure with sequence from Bordetella pertussis Tohama I. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BVGS_BORPE Member of the two-component regulatory system BvgS/BvgA. Phosphorylates BvgA via a four-step phosphorelay in response to environmental signals. 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 Two-component sensory transduction systems control important bacterial programs. In Bordetella pertussis, expression of the virulence regulon is controlled by the unorthodox BvgAS two-component system. BvgS is the prototype of a family of sensor-kinases that harbor periplasmic domains homologous to bacterial solute-binding proteins. Although BvgAS is active under laboratory conditions, no activating signal has been identified, only negative modulators. Here we show that the second periplasmic domain of BvgS interacts with modulators and adopts a Venus flytrap (VFT) fold. X-ray crystallography reveals that the two lobes of VFT2 delimitate a ligand-binding cavity enclosing fortuitous ligands. Most substitutions of putative ligand-binding residues in the VFT2 cavity keep BvgS active, and alteration of the cavity's electrostatic potential affects responsiveness to modulation. The crystal structure of this VFT2 variant conferring constitutive kinase activity to BvgS shows a closed cavity with another nonspecific ligand. Thus, VFT2 is closed and active without a specific agonist ligand, in contrast to typical VFTs. Modulators are antagonists of VFT2 that interrupt signaling. BvgAS is active for most of the B. pertussis infectious cycle, consistent with the proposed mechanism. Periplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanism.,Herrou J, Bompard C, Wintjens R, Dupre E, Willery E, Villeret V, Locht C, Antoine R, Jacob-Dubuisson F Proc Natl Acad Sci U S A. 2010 Sep 20. PMID:20855615 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3mpl, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image