2c1v
From Proteopedia
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|PDB= 2c1v |SIZE=350|CAPTION= <scene name='initialview01'>2c1v</scene>, resolution 1.20Å | |PDB= 2c1v |SIZE=350|CAPTION= <scene name='initialview01'>2c1v</scene>, resolution 1.20Å | ||
|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c1v OCA], [http://www.ebi.ac.uk/pdbsum/2c1v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c1v RCSB]</span> | ||
}} | }} | ||
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[[Category: Echalier, A.]] | [[Category: Echalier, A.]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: HEC]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| - | [[Category: oxidoreductase | + | [[Category: oxidoreductase,periplasmic]] |
| - | + | ||
[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:02 2008'' |
Revision as of 23:15, 30 March 2008
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| , resolution 1.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS- MIXED VALENCE FORM
Overview
Bacterial cytochrome c peroxidases contain an electron transferring (E) heme domain and a peroxidatic (P) heme domain. All but one of these enzymes are isolated in an inactive oxidized state and require reduction of the E heme by a small redox donor protein in order to activate the P heme. Here we present the structures of the inactive oxidized and active mixed valence enzyme from Paracoccus pantotrophus. Chain flexibility in the former, as expressed by the crystallographic temperature factors, is strikingly distributed in certain loop regions, and these coincide with the regions of conformational change that occur in forming the active mixed valence enzyme. On the basis of these changes, we postulate a series of events that occur to link the trigger of the electron entering the E heme from either pseudoazurin or cytochrome c(550) and the dissociation of a coordinating histidine at the P heme, which allows substrate access.
About this Structure
2C1V is a Single protein structure of sequence from Paracoccus pantotrophus. Full crystallographic information is available from OCA.
Reference
Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus., Echalier A, Goodhew CF, Pettigrew GW, Fulop V, Structure. 2006 Jan;14(1):107-17. PMID:16407070
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