2cdv
From Proteopedia
(New page: 200px<br /><applet load="2cdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cdv, resolution 1.8Å" /> '''REFINED STRUCTURE OF ...) |
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| - | [[Image:2cdv.gif|left|200px]]<br /><applet load="2cdv" size=" | + | [[Image:2cdv.gif|left|200px]]<br /><applet load="2cdv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cdv, resolution 1.8Å" /> | caption="2cdv, resolution 1.8Å" /> | ||
'''REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION'''<br /> | '''REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of cytochrome c3 from the sulfate-reducing bacterium | + | The structure of cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio vulgaris Miyazaki has been successfully refined at 1.8 A resolution. The crystallographic R factor is 0.176 for 9907 significant reflections. The isotropic temperature factors of individual atoms were refined and a total of 47 water molecules located on the difference map were incorporated in the refinement. The four heme groups are closely packed, with adjacent pairs of heme planes being nearly perpendicular to each other. The fifth and the sixth ligands of the heme iron atoms are histidine residues with N epsilon 2-Fe distances ranging from 1.88 A to 2.12 A. The histidine co-ordination to the heme iron is different for each heme group. The heme groups are all highly exposed to solvent, although the actual regions exposed differ among the hemes. The four heme groups are located in different environments, and the heme planes are deformed from planarity. The differences in the heme structures and their environments indicate that the four heme groups are non-equivalent. The chemical as well as the physical properties of cytochrome c3 should be interpreted in terms of the structural non-equivalence of the heme groups. The characteristic secondary structural non-equivalence of the heme groups. The characteristic secondary structures of the polypeptide chain of this molecule are three short alpha-helices, two short beta-strands and ten reverse turns. |
==About this Structure== | ==About this Structure== | ||
| - | 2CDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 2CDV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1CDV. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: heme protein of electron transport]] | [[Category: heme protein of electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:48 2008'' |
Revision as of 14:47, 21 February 2008
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REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION
Overview
The structure of cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio vulgaris Miyazaki has been successfully refined at 1.8 A resolution. The crystallographic R factor is 0.176 for 9907 significant reflections. The isotropic temperature factors of individual atoms were refined and a total of 47 water molecules located on the difference map were incorporated in the refinement. The four heme groups are closely packed, with adjacent pairs of heme planes being nearly perpendicular to each other. The fifth and the sixth ligands of the heme iron atoms are histidine residues with N epsilon 2-Fe distances ranging from 1.88 A to 2.12 A. The histidine co-ordination to the heme iron is different for each heme group. The heme groups are all highly exposed to solvent, although the actual regions exposed differ among the hemes. The four heme groups are located in different environments, and the heme planes are deformed from planarity. The differences in the heme structures and their environments indicate that the four heme groups are non-equivalent. The chemical as well as the physical properties of cytochrome c3 should be interpreted in terms of the structural non-equivalence of the heme groups. The characteristic secondary structural non-equivalence of the heme groups. The characteristic secondary structures of the polypeptide chain of this molecule are three short alpha-helices, two short beta-strands and ten reverse turns.
About this Structure
2CDV is a Single protein structure of sequence from Desulfovibrio vulgaris with as ligand. This structure supersedes the now removed PDB entry 1CDV. Full crystallographic information is available from OCA.
Reference
Refined structure of cytochrome c3 at 1.8 A resolution., Higuchi Y, Kusunoki M, Matsuura Y, Yasuoka N, Kakudo M, J Mol Biol. 1984 Jan 5;172(1):109-39. PMID:6319712
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