5uxf

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==Crystal Structure of mouse RECON (AKR1C13) in complex with Cyclic di-AMP==
==Crystal Structure of mouse RECON (AKR1C13) in complex with Cyclic di-AMP==
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<StructureSection load='5uxf' size='340' side='right' caption='[[5uxf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='5uxf' size='340' side='right'caption='[[5uxf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5uxf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UXF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5uxf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UXF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.501&#8491;</td></tr>
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<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=5uxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uxf OCA], [http://pdbe.org/5uxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uxf RCSB], [http://www.ebi.ac.uk/pdbsum/5uxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uxf ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uxf OCA], [https://pdbe.org/5uxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uxf RCSB], [https://www.ebi.ac.uk/pdbsum/5uxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uxf ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/AK1CD_MOUSE AK1CD_MOUSE] Catalyzes the dehydrogenation of 17-beta-hydroxysteroids. May also exhibit significant activity with a variety of cyclic and alicyclic alcohols. Uses both NAD and NADP, but the activity is much greater with NAD than with NADP (By similarity).
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Bacterial and host cyclic dinucleotides (cdNs) mediate cytosolic immune responses through the STING signaling pathway, although evidence suggests that alternative pathways exist. We used cdN-conjugated beads to biochemically isolate host receptors for bacterial cdNs, and we identified the oxidoreductase RECON. High-affinity cdN binding inhibited RECON enzyme activity by simultaneously blocking the substrate and cosubstrate sites, as revealed by structural analyses. During bacterial infection of macrophages, RECON antagonized STING activation by acting as a molecular sink for cdNs. Bacterial infection of hepatocytes, which do not express STING, revealed that RECON negatively regulates NF-kappaB activation. Loss of RECON activity, via genetic ablation or inhibition by cdNs, increased NF-kappaB activation and reduced bacterial survival, suggesting that cdN inhibition of RECON promotes a proinflammatory, antibacterial state that is distinct from the antiviral state associated with STING activation. Thus, RECON functions as a cytosolic sensor for bacterial cdNs, shaping inflammatory gene activation via its effects on STING and NF-kappaB.
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Sensing of Bacterial Cyclic Dinucleotides by the Oxidoreductase RECON Promotes NF-kappaB Activation and Shapes a Proinflammatory Antibacterial State.,McFarland AP, Luo S, Ahmed-Qadri F, Zuck M, Thayer EF, Goo YA, Hybiske K, Tong L, Woodward JJ Immunity. 2017 Mar 21;46(3):433-445. doi: 10.1016/j.immuni.2017.02.014. PMID:28329705<ref>PMID:28329705</ref>
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==See Also==
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*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5uxf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Luo, S]]
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[[Category: Large Structures]]
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[[Category: Tong, L]]
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[[Category: Mus musculus]]
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[[Category: Aldo-keto reductase]]
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[[Category: Luo S]]
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[[Category: Cyclic di-amp]]
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[[Category: Tong L]]
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[[Category: Oxidoreductase]]
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[[Category: Tim barrel]]
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Current revision

Crystal Structure of mouse RECON (AKR1C13) in complex with Cyclic di-AMP

PDB ID 5uxf

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