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1hro
From Proteopedia
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[[Image:1hro.gif|left|200px]] | [[Image:1hro.gif|left|200px]] | ||
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'''MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS''' | '''MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS''' | ||
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[[Category: Holden, H M.]] | [[Category: Holden, H M.]] | ||
[[Category: Meyer, T E.]] | [[Category: Meyer, T E.]] | ||
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Heme]] |
| - | [[Category: | + | [[Category: Photosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:10, 2 May 2008
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. 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 Fri May 2 19:10:03 2008
