6uy5
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli cysteine desulfurase SufS with a spontaneously rotated beta-hairpin== | |
| - | + | <StructureSection load='6uy5' size='340' side='right'caption='[[6uy5]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6uy5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6UY5 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene></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=6uy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uy5 OCA], [http://pdbe.org/6uy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uy5 RCSB], [http://www.ebi.ac.uk/pdbsum/6uy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uy5 ProSAT]</span></td></tr> | ||
| + | </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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dunkle, J A]] | ||
| + | [[Category: Frantom, P A]] | ||
| + | [[Category: Cysteine desulfurase]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Persulfide]] | ||
| + | [[Category: Plp]] | ||
| + | [[Category: Suf]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:23, 27 March 2020
E. coli cysteine desulfurase SufS with a spontaneously rotated beta-hairpin
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Categories: Large Structures | Dunkle, J A | Frantom, P A | Cysteine desulfurase | Lyase | Persulfide | Plp | Suf | Transferase
