1r0h: Difference between revisions
New page: left|200px<br /><applet load="1r0h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r0h, resolution 1.70Å" /> '''cobalt-substituted r... |
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[[Image:1r0h.jpg|left|200px]]<br /><applet load="1r0h" size=" | [[Image:1r0h.jpg|left|200px]]<br /><applet load="1r0h" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1r0h, resolution 1.70Å" /> | caption="1r0h, resolution 1.70Å" /> | ||
'''cobalt-substituted rubredoxin'''<br /> | '''cobalt-substituted rubredoxin'''<br /> | ||
==Overview== | ==Overview== | ||
Five different metal-substituted forms of Clostridium pasteurianum | Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe atom present in the Fe(S-Cys)(4) site of the native form of the protein was exchanged in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin crystallized in space group R3 and were isomorphous with the native protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites with geometries similar to that of the Fe form (effective D(2d) local symmetry), as did the Cd and Hg proteins, but with a significant expansion of the metal-sulfur bond lengths. A knowledge of these structures contributes to a molecular understanding of the function of this simple iron-sulfur electron-transport protein. | ||
==About this Structure== | ==About this Structure== | ||
1R0H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1R0H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0H OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cross, M.]] | [[Category: Cross, M.]] | ||
[[Category: Guss, J | [[Category: Guss, J M.]] | ||
[[Category: Maher, M.]] | [[Category: Maher, M.]] | ||
[[Category: Wedd, A | [[Category: Wedd, A G.]] | ||
[[Category: Wilce, M | [[Category: Wilce, M C.J.]] | ||
[[Category: CO]] | [[Category: CO]] | ||
[[Category: clostridium pasteurianum]] | [[Category: clostridium pasteurianum]] | ||
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[[Category: rubredoxin]] | [[Category: rubredoxin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:38 2008'' | ||
Revision as of 15:45, 21 February 2008
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cobalt-substituted rubredoxin
OverviewOverview
Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe atom present in the Fe(S-Cys)(4) site of the native form of the protein was exchanged in turn for Co, Ni, Ga, Cd and Hg. All five forms of rubredoxin crystallized in space group R3 and were isomorphous with the native protein. The Co-, Ni- and Ga-substituted proteins exhibited metal sites with geometries similar to that of the Fe form (effective D(2d) local symmetry), as did the Cd and Hg proteins, but with a significant expansion of the metal-sulfur bond lengths. A knowledge of these structures contributes to a molecular understanding of the function of this simple iron-sulfur electron-transport protein.
About this StructureAbout this Structure
1R0H is a Single protein structure of sequence from Clostridium pasteurianum with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum., Maher M, Cross M, Wilce MC, Guss JM, Wedd AG, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):298-303. Epub 2004, Jan 23. PMID:14747706
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