5b3t: Difference between revisions
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New page: '''Unreleased structure''' The entry 5b3t is ON HOLD until Paper Publication Authors: Takao, H., Wada, K. Description: Crystal structure of apo-form biliverdin reductase from Synechocy... |
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==Crystal structure of apo-form biliverdin reductase from Synechocystis sp. PCC 6803== | |||
<StructureSection load='5b3t' size='340' side='right'caption='[[5b3t]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5b3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B3T 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]] 2.099Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5b3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b3t OCA], [https://pdbe.org/5b3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b3t RCSB], [https://www.ebi.ac.uk/pdbsum/5b3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b3t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P72782_SYNY3 P72782_SYNY3] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biliverdin reductase catalyses the last step in haem degradation and produces the major lipophilic antioxidant bilirubin via reduction of biliverdin, using NAD(P)H as a cofactor. Despite the importance of biliverdin reductase in maintaining the redox balance, the molecular details of the reaction it catalyses remain unknown. Here we present the crystal structure of biliverdin reductase in complex with biliverdin and NADP+. Unexpectedly, two biliverdin molecules, which we designated the proximal and distal biliverdins, bind with stacked geometry in the active site. The nicotinamide ring of the NADP+ is located close to the reaction site on the proximal biliverdin, supporting that the hydride directly attacks this position of the proximal biliverdin. The results of mutagenesis studies suggest that a conserved Arg185 is essential for the catalysis. The distal biliverdin probably acts as a conduit to deliver the proton from Arg185 to the proximal biliverdin, thus yielding bilirubin. | |||
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity.,Takao H, Hirabayashi K, Nishigaya Y, Kouriki H, Nakaniwa T, Hagiwara Y, Harada J, Sato H, Yamazaki T, Sakakibara Y, Suiko M, Asada Y, Takahashi Y, Yamamoto K, Fukuyama K, Sugishima M, Wada K Nat Commun. 2017 Feb 7;8:14397. doi: 10.1038/ncomms14397. PMID:28169272<ref>PMID:28169272</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Takao | <div class="pdbe-citations 5b3t" style="background-color:#fffaf0;"></div> | ||
[[Category: Wada | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | |||
[[Category: Takao H]] | |||
[[Category: Wada K]] | |||
Latest revision as of 19:25, 29 May 2024
Crystal structure of apo-form biliverdin reductase from Synechocystis sp. PCC 6803
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