1cci
From Proteopedia
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|PDB= 1cci |SIZE=350|CAPTION= <scene name='initialview01'>1cci</scene>, resolution 2.4Å | |PDB= 1cci |SIZE=350|CAPTION= <scene name='initialview01'>1cci</scene>, resolution 2.4Å | ||
|SITE= <scene name='pdbsite=ACT:Removal+Of+PHE+202+Forms+An+Internal+Cavity+Adjacent+To+...'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Removal+Of+PHE+202+Forms+An+Internal+Cavity+Adjacent+To+...'>ACT</scene> | ||
| - | |LIGAND= <scene name='pdbligand=DMI:2,3-DIMETHYLIMIDAZOLIUM+ION'>DMI</scene> | + | |LIGAND= <scene name='pdbligand=DMI:2,3-DIMETHYLIMIDAZOLIUM+ION'>DMI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= CCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= CCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cci OCA], [http://www.ebi.ac.uk/pdbsum/1cci PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cci RCSB]</span> | ||
}} | }} | ||
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[[Category: Musah, R A.]] | [[Category: Musah, R A.]] | ||
[[Category: Wilcox, S K.]] | [[Category: Wilcox, S K.]] | ||
| - | [[Category: DMI]] | ||
| - | [[Category: HEM]] | ||
[[Category: heme]] | [[Category: heme]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:18:59 2008'' |
Revision as of 16:18, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Gene: | CCP (Saccharomyces cerevisiae) | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP
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
1CCI 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 Sun Mar 30 19:18:59 2008
