1duw
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(New page: 200px<br /><applet load="1duw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1duw, resolution 1.89Å" /> '''STRUCTURE OF NONAHEM...)
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Revision as of 01:35, 25 November 2007
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STRUCTURE OF NONAHEME CYTOCHROME C
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.
About this Structure
1DUW is a Single protein structure of sequence from Desulfovibrio desulfuricans with HEM and GOL as ligands. Full crystallographic information is available from OCA.
Reference
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 Sun Nov 25 03:42:46 2007
Categories: Desulfovibrio desulfuricans | Single protein | Breed, J. | Diederichs, K. | Fritz, G. | Kroneck, P.M. | Umhau, S. | Welte, W. | GOL | HEM | Cytochrome c | Electron transport | Heme | Hmc operon | Hydrogenase