1kmk
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kmk RCSB], [http://www.ebi.ac.uk/pdbsum/1kmk PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1kmk TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kmk RCSB], [http://www.ebi.ac.uk/pdbsum/1kmk PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1kmk TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 23:56, 24 December 2014
E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).
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