1yx3
From Proteopedia
(New page: 200px<br /><applet load="1yx3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yx3" /> '''NMR structure of Allochromatium vinosum DsrC...) |
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| - | [[Image:1yx3.gif|left|200px]]<br /><applet load="1yx3" size=" | + | [[Image:1yx3.gif|left|200px]]<br /><applet load="1yx3" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4'''<br /> | '''NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Seven new genes designated dsrLJOPNSR were identified immediately | + | Seven new genes designated dsrLJOPNSR were identified immediately downstream of dsrABEFHCMK, completing the dsr gene cluster of the phototrophic sulfur bacterium Allochromatium vinosum D (DSM 180(T)). Interposon mutagenesis proved an essential role of the encoded proteins for the oxidation of intracellular sulfur, an obligate intermediate during the oxidation of sulfide and thiosulfate. While dsrR and dsrS encode cytoplasmic proteins of unknown function, the other genes encode a predicted NADPH:acceptor oxidoreductase (DsrL), a triheme c-type cytochrome (DsrJ), a periplasmic iron-sulfur protein (DsrO), and an integral membrane protein (DsrP). DsrN resembles cobyrinic acid a,c-diamide synthases and is probably involved in the biosynthesis of siro(heme)amide, the prosthetic group of the dsrAB-encoded sulfite reductase. The presence of most predicted Dsr proteins in A. vinosum was verified by Western blot analysis. With the exception of the constitutively present DsrC, the formation of Dsr gene products was greatly enhanced by sulfide. DsrEFH were purified from the soluble fraction and constitute a soluble alpha(2)beta(2)gamma(2)-structured 75-kDa holoprotein. DsrKJO were purified from membranes pointing at the presence of a transmembrane electron-transporting complex consisting of DsrKMJOP. In accordance with the suggestion that related complexes from dissimilatory sulfate reducers transfer electrons to sulfite reductase, the A. vinosum Dsr complex is copurified with sulfite reductase, DsrEFH, and DsrC. We therefore now have an ideal and unique possibility to study the interaction of sulfite reductase with other proteins and to clarify the long-standing problem of electron transport from and to sulfite reductase, not only in phototrophic bacteria but also in sulfate-reducing prokaryotes. |
==About this Structure== | ==About this Structure== | ||
| - | 1YX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full crystallographic information is available from [http:// | + | 1YX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Allochromatium vinosum]] | [[Category: Allochromatium vinosum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cort, J | + | [[Category: Cort, J R.]] |
[[Category: Dahl, C.]] | [[Category: Dahl, C.]] | ||
| - | [[Category: Kennedy, M | + | [[Category: Kennedy, M A.]] |
| - | [[Category: Montelione, G | + | [[Category: Montelione, G T.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: dissimilatory sulfite reductase]] | [[Category: dissimilatory sulfite reductase]] | ||
[[Category: dsrc]] | [[Category: dsrc]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:03 2008'' |
Revision as of 14:10, 21 February 2008
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NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4
Overview
Seven new genes designated dsrLJOPNSR were identified immediately downstream of dsrABEFHCMK, completing the dsr gene cluster of the phototrophic sulfur bacterium Allochromatium vinosum D (DSM 180(T)). Interposon mutagenesis proved an essential role of the encoded proteins for the oxidation of intracellular sulfur, an obligate intermediate during the oxidation of sulfide and thiosulfate. While dsrR and dsrS encode cytoplasmic proteins of unknown function, the other genes encode a predicted NADPH:acceptor oxidoreductase (DsrL), a triheme c-type cytochrome (DsrJ), a periplasmic iron-sulfur protein (DsrO), and an integral membrane protein (DsrP). DsrN resembles cobyrinic acid a,c-diamide synthases and is probably involved in the biosynthesis of siro(heme)amide, the prosthetic group of the dsrAB-encoded sulfite reductase. The presence of most predicted Dsr proteins in A. vinosum was verified by Western blot analysis. With the exception of the constitutively present DsrC, the formation of Dsr gene products was greatly enhanced by sulfide. DsrEFH were purified from the soluble fraction and constitute a soluble alpha(2)beta(2)gamma(2)-structured 75-kDa holoprotein. DsrKJO were purified from membranes pointing at the presence of a transmembrane electron-transporting complex consisting of DsrKMJOP. In accordance with the suggestion that related complexes from dissimilatory sulfate reducers transfer electrons to sulfite reductase, the A. vinosum Dsr complex is copurified with sulfite reductase, DsrEFH, and DsrC. We therefore now have an ideal and unique possibility to study the interaction of sulfite reductase with other proteins and to clarify the long-standing problem of electron transport from and to sulfite reductase, not only in phototrophic bacteria but also in sulfate-reducing prokaryotes.
About this Structure
1YX3 is a Single protein structure of sequence from Allochromatium vinosum. Full crystallographic information is available from OCA.
Reference
Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum., Dahl C, Engels S, Pott-Sperling AS, Schulte A, Sander J, Lubbe Y, Deuster O, Brune DC, J Bacteriol. 2005 Feb;187(4):1392-404. PMID:15687204
Page seeded by OCA on Thu Feb 21 16:10:03 2008
Categories: Allochromatium vinosum | Single protein | Cort, J R. | Dahl, C. | Kennedy, M A. | Montelione, G T. | NESG, Northeast Structural Genomics Consortium. | Dissimilatory sulfite reductase | Dsrc | Dsvc | Gamma subunit | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Structural genomics
