1hro
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1hro" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hro, resolution 2.2Å" /> '''MOLECULAR STRUCTURE O...)
Next diff →
Revision as of 14:39, 20 November 2007
|
MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS
Overview
Unlike their mitochondrial counterparts, the c-type cytochromes typically, isolated from photosynthetic nonsulfur purple bacteria display a wide, range of oxidation-reduction potentials. Here we describe the X-ray, crystallographic analysis of the cytochrome c2 isolated from Rhodopila, globiformis. This particular c-type cytochrome was selected for study, because of its anomalously high redox potential of +450 mV. Crystals, employed in the investigation belonged to the space group I4(1) with unit, cell dimensions of a = b = 79.2 A, c = 75.2 A, and two molecules in the, asymmetric unit. The structure was solved by the techniques of multiple, isomorphous replacement with two heavy-atom derivatives and electron, density modification procedures. Least-squares refinement of the model, reduced the R-factor to 18.7% for all measured X-ray data from 30.0 to 2.2, A. The overall structural motif of the protein is composed of five, alpha-helices, one type I turn, and six type II turns. As in other, cytochromes c, there are two conserved water molecules located in the, heme-binding pocket. Overall, the three-dimensional structure of the R., globiformis molecule is more similar to the eukaryotic c-type cytochromes, than to other bacterial proteins.
About this Structure
1HRO is a Single protein structure of sequence from Rhodopila globiformis with HEM as ligand. Full crystallographic information is available from OCA.
Reference
Molecular structure of a high potential cytochrome c2 isolated from Rhodopila globiformis., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1996 Sep 15;333(2):338-48. PMID:8809072
Page seeded by OCA on Tue Nov 20 16:47:11 2007
