1cci
From Proteopedia
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| - | [[Image:1cci.gif|left|200px]] | + | [[Image:1cci.gif|left|200px]] |
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| - | '''HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=DMI:2,3-DIMETHYLIMIDAZOLIUM+ION'>DMI</scene> and <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] | ||
| + | |GENE= CCP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CCI is a [ | + | 1CCI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CCI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8673607 8673607] |
[[Category: Cytochrome-c peroxidase]] | [[Category: Cytochrome-c peroxidase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:22:46 2008'' |
Revision as of 08:22, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Gene: | CCP (Saccharomyces cerevisiae) | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| 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 Thu Mar 20 10:22:46 2008
