1duw: Difference between revisions

Revision as of 13:20, 21 February 2008

STRUCTURE OF NONAHEME CYTOCHROME C

OverviewOverview

A nine heme group containing cytochrome c isolated from the soluble and membrane fractions of Desulfovibrio desulfuricans Essex, termed nonaheme cytochrome c, was crystallized, and the structure was solved using the multiple wavelength anomalous dispersion (MAD) phasing method. Refinement was carried out to a resolution of 1.89 A, and anisotropic temperature factors were addressed to the iron and sulfur atoms in the model. The structure revealed two cytochrome c(3) like domains with the typical arrangement of four heme centers. Both domains flanked an extra heme buried under the protein surface. This heme is held in position by loop extensions in each of the two domains. Although both the N- and C-terminal tetraheme domains exhibit a fold and heme arrangement very similar to that of cytochrome c(3), they differ considerably in their loop extensions and electrostatic surface. Analysis of the structure provides evidence for a different function of both domains, namely, anchoring the protein in a transmembranous complex with the N-terminal domain and formation of an electron-transfer complex with hydrogenase by the C-terminal domain.

About this StructureAbout this Structure

1DUW is a Single protein structure of sequence from Desulfovibrio desulfuricans with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the nonaheme cytochrome c from Desulfovibrio desulfuricans Essex in the Fe(III) state at 1.89 A resolution., Umhau S, Fritz G, Diederichs K, Breed J, Welte W, Kroneck PM, Biochemistry. 2001 Feb 6;40(5):1308-16. PMID:11170457

Page seeded by OCA on Thu Feb 21 12:20:42 2008

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OCA

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-[[Image:1duw.jpg|left|200px]]<br /><applet load="1duw" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1duw.jpg|left|200px]]<br /><applet load="1duw" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1duw, resolution 1.89&Aring;" />
 '''STRUCTURE OF NONAHEME CYTOCHROME C'''<br />
 ==Overview==
-A nine heme group containing cytochrome c isolated from the soluble and, membrane fractions of Desulfovibrio desulfuricans Essex, termed nonaheme, cytochrome c, was crystallized, and the structure was solved using the, multiple wavelength anomalous dispersion (MAD) phasing method. Refinement, was carried out to a resolution of 1.89 A, and anisotropic temperature, factors were addressed to the iron and sulfur atoms in the model. The, structure revealed two cytochrome c(3) like domains with the typical, arrangement of four heme centers. Both domains flanked an extra heme, buried under the protein surface. This heme is held in position by loop, extensions in each of the two domains. Although both the N- and C-terminal, tetraheme domains exhibit a fold and heme arrangement very similar to that, of cytochrome c(3), they differ considerably in their loop extensions and, electrostatic surface. Analysis of the structure provides evidence for a, different function of both domains, namely, anchoring the protein in a, transmembranous complex with the N-terminal domain and formation of an, electron-transfer complex with hydrogenase by the C-terminal domain.
+A nine heme group containing cytochrome c isolated from the soluble and membrane fractions of Desulfovibrio desulfuricans Essex, termed nonaheme cytochrome c, was crystallized, and the structure was solved using the multiple wavelength anomalous dispersion (MAD) phasing method. Refinement was carried out to a resolution of 1.89 A, and anisotropic temperature factors were addressed to the iron and sulfur atoms in the model. The structure revealed two cytochrome c(3) like domains with the typical arrangement of four heme centers. Both domains flanked an extra heme buried under the protein surface. This heme is held in position by loop extensions in each of the two domains. Although both the N- and C-terminal tetraheme domains exhibit a fold and heme arrangement very similar to that of cytochrome c(3), they differ considerably in their loop extensions and electrostatic surface. Analysis of the structure provides evidence for a different function of both domains, namely, anchoring the protein in a transmembranous complex with the N-terminal domain and formation of an electron-transfer complex with hydrogenase by the C-terminal domain.
 ==About this Structure==
-DUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DUW OCA].
+DUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUW OCA].
 ==Reference==
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 [[Category: Diederichs, K.]]
 [[Category: Fritz, G.]]
-[[Category: Kroneck, P.M.]]
+[[Category: Kroneck, P M.]]
 [[Category: Umhau, S.]]
 [[Category: Welte, W.]]
@@ Line 27: / Line 27: @@
 [[Category: hydrogenase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:42:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:42 2008''