1azz | pdb_00001azz

FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN

spinqualitylabelsall models 1azz, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1azz is a 4 chain structure with sequence from Celuca pugilator and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: Brachyurin, with EC number 3.4.21.32 Resources: FirstGlance, OCA, RCSB, PDBsum Function [COGS_UCAPU] This enzyme is a serine protease capable of degrading the native triple helix of collagen. [ECOT_ECOLI] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706] 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 crystal structure of fiddler crab collagenase complexed with the dimeric serine protease inhibitor ecotin at 2.5 A resolution reveals an extended cleft providing binding sites for at least 11 contiguous substrate residues. Comparison of the positions of nine intermolecular main chain hydrogen bonding interactions in the cleft, with the known sequences at the cleavage site of type I collagen, suggests that the protease binding loop of ecotin adopts a conformation mimicking that of the cleaved strand of collagen. A well-defined groove extending across the binding surface of the enzyme readily accommodates the two other polypeptide chains of the triple-helical substrate. These observations permit construction of a detailed molecular model for collagen recognition and cleavage by this invertebrate serine protease. Ecotin undergoes a pronounced internal structural rearrangement which permits binding in the observed conformation. The capacity for such rearrangement appears to be a key determinant of its ability to inhibit a wide range of serine proteases. Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix.,Perona JJ, Tsu CA, Craik CS, Fletterick RJ Biochemistry. 1997 May 6;36(18):5381-92. PMID:9154920 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ecotin

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