1hb0 | pdb_00001hb0

Snapshots of serine protease catalysis: (D) acyl-enzyme intermediate between porcine pancreatic elastase and human beta-casomorphin-7 jumped to pH 10 for 2 minutes

spinqualitylabelsall models 1hb0, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hb0 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, SO4 Related: 1b0e, 1bma, 1btu, 1c1m, 1e34, 1e35, 1e36, 1e37, 1e38, 1eai, 1eas, 1eat, 1eau, 1ela, 1elb, 1elc, 1eld, 1ele, 1elf, 1elg, 1esa, 1esb, 1est, 1fle, 1h9l, 1hv7, 1inc, 1jim, 1lvy, 1nes, 1qgf, 1qix, 1qnj, 1qr3, 2est, 3est, 4est, 5est, 6est, 7est, 8est, 9est, 1hax, 1hay, 1haz Activity: Hydrolase, with EC number and 3.4.21.37 3.4.21.36 and 3.4.21.37 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CELA1_PIG] Acts upon elastin. 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 Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site. X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate.,Wilmouth RC, Edman K, Neutze R, Wright PA, Clifton IJ, Schneider TR, Schofield CJ, Hajdu J Nat Struct Biol. 2001 Aug;8(8):689-94. PMID:11473259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elastase 3D structures

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