1ryc
From Proteopedia
(New page: 200px<br /><applet load="1ryc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryc, resolution 1.8Å" /> '''CYTOCHROME C PEROXIDA...) |
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| - | [[Image:1ryc.jpg|left|200px]]<br /><applet load="1ryc" size=" | + | [[Image:1ryc.jpg|left|200px]]<br /><applet load="1ryc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ryc, resolution 1.8Å" /> | caption="1ryc, resolution 1.8Å" /> | ||
'''CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE'''<br /> | '''CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Conformational changes that gate the access of substrates or ligands to an | + | 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 Structure== | ==About this Structure== | ||
| - | 1RYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with HEM and BZI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http:// | + | 1RYC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=BZI:'>BZI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fitzgerald, M | + | [[Category: Fitzgerald, M M.]] |
| - | [[Category: Goodin, D | + | [[Category: Goodin, D B.]] |
| - | [[Category: Mcree, D | + | [[Category: Mcree, D E.]] |
[[Category: Musah, R.]] | [[Category: Musah, R.]] | ||
[[Category: BZI]] | [[Category: BZI]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:53 2008'' |
Revision as of 12:55, 21 February 2008
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CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE
Overview
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 Structure
1RYC is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 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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