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1pq5

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{{STRUCTURE_1pq5| PDB=1pq5 | SCENE= }}
{{STRUCTURE_1pq5| PDB=1pq5 | SCENE= }}
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'''Trypsin at pH 5, 0.85 A'''
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===Trypsin at pH 5, 0.85 A===
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==Overview==
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A series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor, were determined at atomic and ultra-high resolution and subjected to ab initio quantum chemical calculations and multipole refinement. Quantum chemical calculations reproduced the observed active site crystal structure with severe deviations from standard stereochemistry and indicated the protonation state of the catalytic residues. Multipole refinement directly revealed the charge distribution in the active site and proved the validity of the ab initio calculations. The combined results confirmed the catalytic function of the active site residues and the two water molecules acting as the nucleophile and the proton donor. The crystal structures represent snapshots from the reaction pathway, close to a tetrahedral intermediate. The de-acylation of trypsin then occurs in true SN2 fashion.
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{{ABSTRACT_PUBMED_12937176}}
==About this Structure==
==About this Structure==
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[[Category: Trypsin]]
[[Category: Trypsin]]
[[Category: Ultra-high resolution]]
[[Category: Ultra-high resolution]]
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Revision as of 12:12, 29 July 2008

Image:1pq5.png

Template:STRUCTURE 1pq5

Trypsin at pH 5, 0.85 A

Template:ABSTRACT PUBMED 12937176

About this Structure

1PQ5 is a Single protein structure of sequence from Fusarium oxysporum. Full crystallographic information is available from OCA.

Reference

Trypsin revisited: crystallography AT (SUB) atomic resolution and quantum chemistry revealing details of catalysis., Schmidt A, Jelsch C, Ostergaard P, Rypniewski W, Lamzin VS, J Biol Chem. 2003 Oct 31;278(44):43357-62. Epub 2003 Aug 22. PMID:12937176

Page seeded by OCA on Tue Jul 29 15:12:08 2008

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