5xt6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==A sulfur-transferring catalytic intermediate of SufS-SufU complex from Bacillus subtilis== | |
| - | + | <StructureSection load='5xt6' size='340' side='right' caption='[[5xt6]], [[Resolution|resolution]] 3.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5xt6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XT6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PDA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC+ACID'>PDA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_desulfurase Cysteine desulfurase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.7 2.8.1.7] </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=5xt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xt6 OCA], [http://pdbe.org/5xt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xt6 RCSB], [http://www.ebi.ac.uk/pdbsum/5xt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xt6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SUFU_BACSU SUFU_BACSU]] Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21236255</ref> <ref>PMID:21744456</ref> <ref>PMID:24321018</ref> [[http://www.uniprot.org/uniprot/SUFS_BACSU SUFS_BACSU]] Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40-to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.<ref>PMID:20097860</ref> <ref>PMID:20822158</ref> <ref>PMID:21744456</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cysteine desulfurase]] | ||
| + | [[Category: Fujishiro, T]] | ||
| + | [[Category: Kunichika, K]] | ||
| + | [[Category: Takahashi, Y]] | ||
| + | [[Category: Biosynthetic protein]] | ||
| + | [[Category: Iron-sulfur cluster biosynthesis]] | ||
| + | [[Category: Metalloprotein]] | ||
| + | [[Category: Suf machinery]] | ||
| + | [[Category: Sulfur mobilization]] | ||
Revision as of 06:21, 20 December 2017
A sulfur-transferring catalytic intermediate of SufS-SufU complex from Bacillus subtilis
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