4dcb

Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11

spinqualitylabelsall models 4dcb, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dcb is a 2 chain structure with sequence from Homo sapiens and Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.033Å Ligands: C8E, MPD, MRD, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLA_YERPE In the mammalian host activates (cleaves) plasminogen to generate the serine protease plasmin. Plasmin degrades fibrin clots (fibrinolysis) and facilitates bacterial cell migration, enabling rapid dissemination of bacteria from the initial site of infection (Probable). Cleaves host plasminogen to generate plasmin and probably also has autocatalytic activity (PubMed:20637417, PubMed:22645135). Fibrinolytic activity prevails at 37 degrees Celsius whereas coagulase expression predominates at lower temperatures (28 degrees Celsius) (PubMed:2526282). Cleaves plasminogen; plasminogen cleavage is much higher than coagulase activity (PubMed:20637417, PubMed:22645135, PubMed:2526282, PubMed:2651310). Publication Abstract from PubMed Omptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity. Structural basis for activation of an integral membrane protease by lipopolysaccharide.,Eren E, van den Berg B J Biol Chem. 2012 Jul 6;287(28):23971-6. Epub 2012 May 29. PMID:22645135 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Plasminogen activator

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