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5db5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21== | |
| + | <StructureSection load='5db5' size='340' side='right'caption='[[5db5]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5db5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH5alpha Escherichia coli DH5alpha]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DB5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5db5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5db5 OCA], [https://pdbe.org/5db5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5db5 RCSB], [https://www.ebi.ac.uk/pdbsum/5db5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5db5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | ||
| - | + | ==See Also== | |
| - | + | *[[Cysteine desulfurase 3D structures|Cysteine desulfurase 3D structures]] | |
| - | + | *[[Selenocysteine lyase|Selenocysteine lyase]] | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Arbing MA]] |
| + | [[Category: Eisenberg D]] | ||
| + | [[Category: Koo CW]] | ||
| + | [[Category: Medrano-Soto A]] | ||
| + | [[Category: Shin A]] | ||
Current revision
Crystal structure of PLP-bound E. coli SufS (cysteine persulfide intermediate) in space group P21
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