7xen
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SufS with L-penicillamine== | |
| + | <StructureSection load='7xen' size='340' side='right'caption='[[7xen]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7xen]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XEN 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]] 2.47Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9ZN:(2~{R})-3-methyl-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-sulfanyl-butanoic+acid'>9ZN</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=7xen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xen OCA], [https://pdbe.org/7xen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xen RCSB], [https://www.ebi.ac.uk/pdbsum/7xen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xen ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The reactivity of pyridoxal-5'-phosphate (PLP) with cysteine and its derivatives has been of increasing interest because the corresponding product, a thiazolidine PLP-cysteine adduct, can be formed via PLP-dependent enzymatic and non-enzymatic reactions. Here, we report biochemical and X-ray crystallographic snapshots of thiazolidine formation in reaction of D-cysteine with PLP in SufS, a PLP-dependent L-cysteine desulfurase. By comparing L- and D-penicillamine-bound SufS showing no thiazolidine formation in the crystals with D-cysteine SufS, we proposed a thiazolidine formation mechanism with important factors: the polar environments provided by the carbonyl groups of Ala28-Ala29 and Lys224-mediated base catalysis for the nucleophilic thiolate of D-cysteine. | ||
| - | + | Visualizing thiazolidine ring formation in the reaction of D-cysteine and pyridoxal-5'-phosphate within L-cysteine desulfurase SufS.,Nakamura R, Fujishiro T Biochem Biophys Res Commun. 2025 Mar 25;754:151497. doi: , 10.1016/j.bbrc.2025.151497. Epub 2025 Feb 19. PMID:40020322<ref>PMID:40020322</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7xen" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fujishiro T]] | ||
| + | [[Category: Nakamura R]] | ||
Current revision
SufS with L-penicillamine
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