1hro

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[[Image:1hro.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hro OCA], [http://www.ebi.ac.uk/pdbsum/1hro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hro RCSB]</span>
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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.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: photosynthesis]]
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[[Category: Photosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:10:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:34 2008''
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Revision as of 16:10, 2 May 2008

Image:1hro.gif

Template:STRUCTURE 1hro

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

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