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1kmk

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[[Image:1kmk.png|left|200px]]
 
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{{STRUCTURE_1kmk| PDB=1kmk | SCENE= }}
{{STRUCTURE_1kmk| PDB=1kmk | SCENE= }}
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===E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).===
===E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).===
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{{ABSTRACT_PUBMED_11827487}}
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{{ABSTRACT_PUBMED_11827487}}
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==Function==
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[[http://www.uniprot.org/uniprot/SUFS_ECOLI SUFS_ECOLI]] Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.<ref>PMID:10829016</ref> <ref>PMID:12089140</ref> <ref>PMID:11997471</ref> <ref>PMID:12876288</ref> <ref>PMID:12941942</ref>
==About this Structure==
==About this Structure==
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[[1kmk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA].
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[[1kmk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:011827487</ref><references group="xtra"/>
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<ref group="xtra">PMID:011827487</ref><references group="xtra"/><references/>
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[[Category: Escherichia coli]]
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[[Category: Bacillus coli migula 1895]]
[[Category: Selenocysteine lyase]]
[[Category: Selenocysteine lyase]]
[[Category: Burley, S K.]]
[[Category: Burley, S K.]]

Revision as of 04:52, 9 April 2014

Template:STRUCTURE 1kmk

Contents

E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).

Template:ABSTRACT PUBMED 11827487

Function

[SUFS_ECOLI] Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.[1] [2] [3] [4] [5]

About this Structure

1kmk is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA.

Reference

  • Lima CD. Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation. J Mol Biol. 2002 Feb 1;315(5):1199-208. PMID:11827487 doi:10.1006/jmbi.2001.5308
  1. ↑ Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000 Aug 4;275(31):23769-73. PMID:10829016 doi:10.1074/jbc.M000926200
  2. ↑ Takahashi Y, Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem. 2002 Aug 9;277(32):28380-3. Epub 2002 Jun 27. PMID:12089140 doi:http://dx.doi.org/10.1074/jbc.C200365200
  3. ↑ Mihara H, Kato S, Lacourciere GM, Stadtman TC, Kennedy RA, Kurihara T, Tokumoto U, Takahashi Y, Esaki N. The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6679-83. Epub 2002 May 7. PMID:11997471 doi:http://dx.doi.org/10.1073/pnas.102176099
  4. ↑ Loiseau L, Ollagnier-de-Choudens S, Nachin L, Fontecave M, Barras F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem. 2003 Oct 3;278(40):38352-9. Epub 2003 Jul 21. PMID:12876288 doi:http://dx.doi.org/10.1074/jbc.M305953200
  5. ↑ Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. PMID:12941942 doi:http://dx.doi.org/10.1074/jbc.M308004200

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