1hro
From Proteopedia
(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...) |
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| - | [[Image:1hro.gif|left|200px]]<br /><applet load="1hro" size=" | + | [[Image:1hro.gif|left|200px]]<br /><applet load="1hro" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hro, resolution 2.2Å" /> | caption="1hro, resolution 2.2Å" /> | ||
'''MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS'''<br /> | '''MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Unlike their mitochondrial counterparts, the c-type cytochromes typically | + | 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== | ==About this Structure== | ||
| - | 1HRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopila_globiformis Rhodopila globiformis] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HRO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodopila_globiformis Rhodopila globiformis] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhodopila globiformis]] | [[Category: Rhodopila globiformis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Benning, M | + | [[Category: Benning, M M.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Meyer, T | + | [[Category: Meyer, T E.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:12 2008'' |
Revision as of 11:04, 21 February 2008
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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 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
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