3dpm

Structure of mature CPAF complexed with lactacystin

spinqualitylabelsall models 3dpm, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3dpm is a 2 chain structure with sequence from Chlamydia trachomatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: LAS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y858_CHLTR 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 The obligate intracellular pathogen Chlamydia trachomatis is the most common cause of sexually transmitted bacterial disease. It secretes a protease known as chlamydial protease/proteasome-like activity factor (CPAF) that degrades many host molecules and plays a major role in Chlamydia pathogenesis. Here, we show that mature CPAF is a homodimer of the catalytic domains, each of which comprises two distinct subunits. Dormancy of the CPAF zymogen is maintained by an internal inhibitory segment that binds the CPAF active site and blocks its homodimerization. CPAF activation is initiated by trans-autocatalytic cleavage, which induces homodimerization and conformational changes that assemble the catalytic triad. This assembly leads to two autocatalytic cleavages and removal of the inhibitory segment, enabling full CPAF activity. CPAF is covalently bound and inhibited by the proteasome inhibitor lactacystin. These results reveal the activation mechanism of the CPAF serine protease and suggest new opportunities for anti-Chlamydia drug development. Structural basis for activation and inhibition of the secreted chlamydia protease CPAF.,Huang Z, Feng Y, Chen D, Wu X, Huang S, Wang X, Xiao X, Li W, Huang N, Gu L, Zhong G, Chai J Cell Host Microbe. 2008 Dec 11;4(6):529-42. PMID:19064254 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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