4lw4
From Proteopedia
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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=4lw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lw4 RCSB], [http://www.ebi.ac.uk/pdbsum/4lw4 PDBsum]</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=4lw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lw4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lw4 RCSB], [http://www.ebi.ac.uk/pdbsum/4lw4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CSDA_ECOLI CSDA_ECOLI]] Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. L-cysteine sulfinic acid is the best substrate. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate.<ref>PMID:10829016</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 23:51, 24 December 2014
Structural changes during cysteine desulfurase CsdA and sulfur-acceptor CsdE interactions provide insight into the trans-persulfuration
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