2C1V

CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS - Mixed VALENCE FORM

Summary for 2C1V

• Entry DOI: 10.2210/pdb2c1v/pdb
• Related: 2C1U
• Descriptor: DI-HAEM CYTOCHROME C PEROXIDASE, HEME C, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: electron transport, heme, oxidoreductase, periplasmic, peroxidase
• Biological source: PARACOCCUS PANTOTROPHUS
• Total number of polymer chains: 2
• Total formula weight: 75455.49

Authors

Echalier, A.,Fulop, V. (deposition date: 2005-09-21, release date: 2006-01-13, Last modification date: 2024-10-16)

Primary citation

Echalier, A.,Goodhew, C.F.,Pettigrew, G.W.,Fulop, V.
Activation and Catalysis of the Di-Heme Cytochrome C Peroxidase from Paracoccus Pantotrophus
Structure, 14:107-, 2006

PubMed Abstract: 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.

PubMed: 16407070
DOI: 10.1016/J.STR.2005.09.011

Experimental method

X-RAY DIFFRACTION (1.2 Å)