1JDL : Structure of cytochrome c2 from Rhodospirillum Centenum

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.7
Classification:ELECTRON TRANSPORT
Release Date:2001-11-07
Deposition Date:2001-06-14
Revision Date:2008-04-27#2011-07-13
Molecular Weight:13669.23
Macromolecule Type:Protein
Residue Count:121
Atom Site Count:935
DOI:10.2210/pdb1jdl/pdb

Abstract:
Cytochrome c(2) from the purple photosynthetic bacterium Rhodospirillum centenum has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 29.7, b = 59.9, c = 65.4 A, and diffract to a resolution limit of 1.7 A. The Fe-atom position was determined from its anomalous scattering contribution and a molecular-replacement solution was calculated. The correctness of the solution was confirmed by parallel isomorphous replacement studies. The resulting model has a type I cytochrome fold with two features, an extended alpha-helix and a surface-charge distribution, that are distinctive to this protein. The implications of these structural features for the ability of the cytochrome to serve as an electron carrier are discussed.
Date made availableNov 7 2001
PublisherRCSB-PDB

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