1yx3: Difference between revisions

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[[Image:1yx3.~~gif~~|left|200px]]

[[Image:1yx3.png|left|200px]]

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~~'''~~NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4~~'''~~

===NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_15687204}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15687204 is the PubMed ID number.

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==About this Structure==

1YX3 is a [[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].

1YX3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX3 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:[http://www.ncbi.nlm.nih.gov/pubmed/15687204 15687204]

Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur., Pott AS, Dahl C, Microbiology. 1998 Jul;144 ( Pt 7):1881-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9695921 9695921]

[[Category: Allochromatium vinosum]]

[[Category: Single protein]]

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[[Category: Psi]]

[[Category: Structural genomic]]

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-[[Image:1yx3.gif|left|200px]]
+{{Seed}}
+[[Image:1yx3.png|left|200px]]
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 {{STRUCTURE_1yx3|  PDB=1yx3  |  SCENE=  }}
-'''NMR structure of Allochromatium vinosum DsrC: Northeast Structural Genomics Consortium target OP4'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15687204}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15687204 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15687204}}
 ==About this Structure==
-YX3 is a [[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].
+YX3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YX3 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:[http://www.ncbi.nlm.nih.gov/pubmed/15687204 15687204]
+Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur., Pott AS, Dahl C, Microbiology. 1998 Jul;144 ( Pt 7):1881-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9695921 9695921]
 [[Category: Allochromatium vinosum]]
 [[Category: Single protein]]
@@ Line 36: / Line 42: @@
 [[Category: Psi]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:54:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Sep 28 19:04:30 2008''