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1sgc

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{{STRUCTURE_1sgc| PDB=1sgc | SCENE= }}
{{STRUCTURE_1sgc| PDB=1sgc | SCENE= }}
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'''THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES'''
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===THE 1.8 ANGSTROMS STRUCTURE OF THE COMPLEX BETWEEN CHYMOSTATIN AND STREPTOMYCES GRISEUS PROTEASE A. A MODEL FOR SERINE PROTEASE CATALYTIC TETRAHEDRAL INTERMEDIATES===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 3892018 is the PubMed ID number.
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{{ABSTRACT_PUBMED_3892018}}
==About this Structure==
==About this Structure==
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[[Category: Brayer, G D.]]
[[Category: Brayer, G D.]]
[[Category: Delbaere, L T.J.]]
[[Category: Delbaere, L T.J.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:40:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:25:05 2008''

Revision as of 07:25, 28 July 2008

Image:1sgc.png

Template:STRUCTURE 1sgc

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

Template:ABSTRACT PUBMED 3892018

About this Structure

1SGC is a Single protein structure of sequence from Streptomyces griseus. Full crystallographic information is available from OCA.

Reference

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

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