2c1v
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Bacterial cytochrome c peroxidases contain an electron transferring (E) | + | 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== | ==About this Structure== | ||
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[[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 Thu Feb 21 16:43:58 2008'' |
Revision as of 14:43, 21 February 2008
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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 with , and as ligands. Active as Cytochrome-c peroxidase, with EC number 1.11.1.5 Known structural/functional Site: . 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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