1ac4

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[[Image:1ac4.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1ac4| PDB=1ac4 | SCENE= }}
{{STRUCTURE_1ac4| PDB=1ac4 | SCENE= }}
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'''VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)'''
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===VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)===
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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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The line below this paragraph, {{ABSTRACT_PUBMED_8673607}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8673607 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8673607}}
==About this Structure==
==About this Structure==
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[[Category: Peroxidase]]
[[Category: Peroxidase]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:05:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:33:34 2008''

Revision as of 13:33, 30 June 2008

Image:1ac4.png

Template:STRUCTURE 1ac4

VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (2,3,4-TRIMETHYL-1,3-THIAZOLE)

Template:ABSTRACT PUBMED 8673607

About this Structure

1AC4 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

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