1ryc

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{{STRUCTURE_1ryc| PDB=1ryc | SCENE= }}
{{STRUCTURE_1ryc| PDB=1ryc | SCENE= }}
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'''CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE'''
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===CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE===
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==Overview==
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Conformational changes that gate the access of substrates or ligands to an active site are important features of enzyme function. In this report, we describe an unusual example of a structural rearrangement near a buried artificial cavity in cytochrome c peroxidase that occurs on binding protonated benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a large solvent-accessible channel for the entry of ligands to an otherwise inaccessible binding site. The trapping of this alternate conformational state provides a unique view of the extent to which protein dynamics can allow small molecule penetration into buried protein cavities.
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{{ABSTRACT_PUBMED_8673607}}
==About this Structure==
==About this Structure==
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[[Category: Musah, R.]]
[[Category: Musah, R.]]
[[Category: Oxidoreductase]]
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Revision as of 21:36, 27 July 2008

Image:1ryc.png

Template:STRUCTURE 1ryc

CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE

Template:ABSTRACT PUBMED 8673607

About this Structure

1RYC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity., Fitzgerald MM, Musah RA, McRee DE, Goodin DB, Nat Struct Biol. 1996 Jul;3(7):626-31. PMID:8673607

Page seeded by OCA on Mon Jul 28 00:36:09 2008

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