4q75: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q75 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q75 RCSB], [http://www.ebi.ac.uk/pdbsum/4q75 PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q75 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q75 RCSB], [http://www.ebi.ac.uk/pdbsum/4q75 PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The chloroplastic Arabidopsis thaliana Nfs2 (AtNfs2) is a group II pyridoxal 5'-phosphate-dependent cysteine desulfurase that is involved in the initial steps of iron-sulfur cluster biogenesis. The group II cysteine desulfurases require the presence of sulfurtransferases such as SufE proteins for optimal activity. Compared with group I cysteine desulfurases, proteins of this group contains a smaller extended lobe harbouring the catalytic cysteine and have a beta-hairpin constraining the active site. Here, two crystal structures of AtNfs2 are reported: a wild-type form with the catalytic cysteine in a persulfide-intermediate state and a C384S variant mimicking the resting state of the enzyme. In both structures the well conserved Lys241 covalently binds pyridoxal 5'-phosphate, forming an internal aldimine. Based on available homologous bacterial complexes, a model of a complex between AtNfs2 and the SufE domain of its biological partner AtSufE1 is proposed, revealing the nature of the binding sites. | |||
X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.,Roret T, Pegeot H, Couturier J, Mulliert G, Rouhier N, Didierjean C Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1180-5. doi:, 10.1107/S2053230X14017026. Epub 2014 Aug 29. PMID:25195888<ref>PMID:25195888</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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