1ac8: Difference between revisions
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'''VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)''' | '''VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)''' | ||
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[[Category: Musah, R A.]] | [[Category: Musah, R A.]] | ||
[[Category: Rosenfeld, R.]] | [[Category: Rosenfeld, R.]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Peroxidase]] | ||
[[Category: | [[Category: Transit peptide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:05:35 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 10:05, 2 May 2008
VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)
OverviewOverview
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.
About this StructureAbout this Structure
1AC8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 10:05:35 2008