6t87

From Proteopedia

(Difference between revisions)

Current revision

Urocanate reductase in complex with urocanate

Structural highlights

6t87 is a 1 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.56Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bogachev AV, Bertsova YV, Bloch DA, Verkhovsky MI. Urocanate reductase: identification of a novel anaerobic respiratory pathway in Shewanella oneidensis MR-1. Mol Microbiol. 2012 Dec;86(6):1452-63. doi: 10.1111/mmi.12067. Epub 2012 Nov 1. PMID:23078170 doi:http://dx.doi.org/10.1111/mmi.12067
↑ Venskutonyte R, Koh A, Stenstrom O, Khan MT, Lundqvist A, Akke M, Backhed F, Lindkvist-Petersson K. Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. Nat Commun. 2021 Mar 1;12(1):1347. doi: 10.1038/s41467-021-21548-y. PMID:33649331 doi:http://dx.doi.org/10.1038/s41467-021-21548-y

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6t87"

Categories: Large Structures | Shewanella oneidensis MR-1 | Lindkvist-Petersson K | Venskutonyte R

@@ Line 3: / Line 3: @@
 <StructureSection load='6t87' size='340' side='right'caption='[[6t87]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[6t87]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. 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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</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='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='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>
 == 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>
+[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 ==
@@ Line 24: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Oxidoreductase]]
+[[Category: Shewanella oneidensis MR-1]]
-[[Category: Lindkvist-Petersson, K]]
+[[Category: Lindkvist-Petersson K]]
-[[Category: Venskutonyte, R]]
+[[Category: Venskutonyte R]]
-[[Category: Bacterial enzyme]]
-[[Category: Urocanate reductase]]

6t87

From Proteopedia

Current revision

Urocanate reductase in complex with urocanate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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