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''' | + | {{Structure |
| + | |PDB= 1hro |SIZE=350|CAPTION= <scene name='initialview01'>1hro</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HRO is a [ | + | 1HRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopila_globiformis Rhodopila globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8809072 8809072] |
[[Category: Rhodopila globiformis]] | [[Category: Rhodopila globiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:50 2008'' |
Revision as of 09:40, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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