1sgc | pdb_00001sgc

THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES

spinqualitylabelsall models 1sgc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sgc is a 2 chain structure with sequence from "actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: CSI, PHA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PRTA_STRGR] Has a primary specificity for large aliphatic or aromatic amino acids. 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 naturally occurring serine protease inhibitor, chymostatin, forms a hemiacetal adduct with the catalytic Ser195 residue of Streptomyces griseus protease A. Restrained parameter least-squares refinement of this complex to 1.8 A resolution has produced an R index of 0 X 123 for the 11,755 observed reflections. The refined distance of the carbonyl carbon atom of the aldehyde to O gamma of Ser195 is 1 X 62 A. Both the R and S configurations of the hemiacetal occur in equal populations, with the end result resembling the expected configuration for a covalent tetrahedral product intermediate of a true substrate. This study strengthens the concept that serine proteases stabilize a covalent, tetrahedrally co-ordinated species and elaborates those features of the enzyme responsible for this effect. We propose that a major driving force for the hydrolysis of peptide bonds by serine proteases is the non-planar distortion of the scissile bond by the enzyme, which thereby lowers the activation energy barrier to hydrolysis by eliminating the resonance stabilization energy of the peptide bond. The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates.,Delbaere LT, Brayer GD J Mol Biol. 1985 May 5;183(1):89-103. PMID:3892018 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proteinase

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