3itf

Structural basis for the inhibitory function of the CPXP adaptor protein

spinqualitylabelsall models 3itf, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3itf is a 2 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPXP_ECOLI Aids in combating extracytoplasmic protein-mediated toxicity. Publication Abstract from PubMed Bacteria are equipped with two- component systems to cope with environmental changes and auxiliary proteins provide response to additional stimuli. The Cpx-two component-system is the global modulator of cell envelope-stress in Gram-negative bacteria that integrates very different signals and consists of the kinase CpxA, the regulator CpxR and the dual function auxiliary protein CpxP. CpxP both inhibits activation of CpxA and is indispensable for the quality control system of P pili that are crucial for uropathogenic Escherichia coli (UEPEC) during kidney colonization. How these two essential biological functions of CpxP are linked is not known. Here, we report the crystal structure of CpxP at 1.45 A resolution with two monomers being interdigitated like left hands forming a cap-shaped dimer. Our combined structural and functional studies suggest that CpxP inhibits the kinase CpxA through direct interaction between its concave polar surface and the negatively charged sensor domain on CpxA. Moreover, an extended hydrophobic cleft on the convex surface suggests a potent substrate recognition site for misfolded pilus subunits. Altogether, the structural details of CpxP provide a first insight how a periplasmic two-component system inhibitor blocks its cognate kinase and is released from it. Structural basis for two-component system inhibition and pilus sensing by the auxiliary CpxP protein.,Zhou X, Keller R, Volkmer R, Krauss N, Scheerer P, Hunke S J Biol Chem. 2011 Jan 14. PMID:21239493 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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