1ryc: Difference between revisions

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[[Image:1ryc.jpg|left|200px]]
{{Seed}}
[[Image:1ryc.png|left|200px]]


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{{STRUCTURE_1ryc|  PDB=1ryc  |  SCENE=  }}  
{{STRUCTURE_1ryc|  PDB=1ryc  |  SCENE=  }}  


'''CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE'''
===CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_8673607}}, adds the Publication Abstract to the page
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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]]
[[Category: Oxidoreductase]]
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