6t87
From Proteopedia
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==Urocanate reductase in complex with urocanate== | ==Urocanate reductase in complex with urocanate== | ||
| - | <StructureSection load='6t87' size='340' side='right'caption='[[6t87]]' scene=''> | + | <StructureSection load='6t87' size='340' side='right'caption='[[6t87]], [[Resolution|resolution]] 1.56Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T87 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t87]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T87 FirstGlance]. <br> |
| - | </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=6t87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t87 OCA], [https://pdbe.org/6t87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t87 RCSB], [https://www.ebi.ac.uk/pdbsum/6t87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t87 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=URO:(2E)-3-(1H-IMIDAZOL-4-YL)ACRYLIC+ACID'>URO</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.33 1.3.99.33] </span></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=6t87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t87 OCA], [https://pdbe.org/6t87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t87 RCSB], [https://www.ebi.ac.uk/pdbsum/6t87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t87 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/URDA_SHEON URDA_SHEON]] Catalyzes the two-electron reduction of urocanate to dihydrourocanate (also named imidazole propionate or deamino-histidine). The physiological electron donor is unknown; it might be the membrane-bound tetraheme cytochrome c (CymA). Enables anaerobic growth with urocanate as a sole terminal electron acceptor, and thus can provide the cells with a niche where no other bacteria can compete and survive. Is unable to reduce cinnamate and other unsaturated organic acids such as acrylic, crotonic, fumaric and orotic acids. Has no fumarate reductase or succinate dehydrogenase activity.<ref>PMID:23078170</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes. | ||
| + | |||
| + | Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production.,Venskutonyte R, Koh A, Stenstrom O, Khan MT, Lundqvist A, Akke M, Backhed F, Lindkvist-Petersson K Nat Commun. 2021 Mar 1;12(1):1347. doi: 10.1038/s41467-021-21548-y. PMID:33649331<ref>PMID:33649331</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6t87" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Lindkvist-Petersson K]] | + | [[Category: Oxidoreductase]] |
| - | [[Category: Venskutonyte R]] | + | [[Category: Lindkvist-Petersson, K]] |
| + | [[Category: Venskutonyte, R]] | ||
| + | [[Category: Bacterial enzyme]] | ||
| + | [[Category: Urocanate reductase]] | ||
Revision as of 17:48, 10 March 2021
Urocanate reductase in complex with urocanate
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