5b4i: Difference between revisions
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==Crystal structure of I86D mutant of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin (data 2)== | |||
<StructureSection load='5b4i' size='340' side='right'caption='[[5b4i]], [[Resolution|resolution]] 1.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5b4i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B4I 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]] 1.11Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</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=5b4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b4i OCA], [https://pdbe.org/5b4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b4i RCSB], [https://www.ebi.ac.uk/pdbsum/5b4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b4i ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PCYA_SYNY3 PCYA_SYNY3] Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the reduction of biliverdin (BV) to produce phycocyanobilin, a linear tetrapyrrole pigment used for light harvesting and light sensing. Spectroscopic and HPLC analyses inidicate that BV bound to the I86D mutant of PcyA is fully protonated (BVH+ ) and can accept an electron, but I86D is unable to donate protons for the reduction; therefore, compared to the wild-type PcyA, the I86D mutant stabilizes BVH+ . To elucidate the structural basis of the I86D mutation, we determined the atomic-resolution structure of the I86D-BVH+ complex and the protonation states of the essential residues Asp105 and Glu76 in PcyA. Our study revealed that Asp105 adopted a fixed conformation in the I86D mutant, although it had dual conformations in wild-type PcyA which reflected the protonation states of BV. Taken together with biochemical/spectroscopic results, our analysis of the I86D-BVH+ structure supports the hypothesis that flexibility of Asp105 is essential for the catalytic activity of PcyA. | |||
Atomic-resolution structure of the phycocyanobilin:ferredoxin oxidoreductase I86D mutant in complex with fully protonated biliverdin.,Hagiwara Y, Wada K, Irikawa T, Sato H, Unno M, Yamamoto K, Fukuyama K, Sugishima M FEBS Lett. 2016 Oct;590(19):3425-3434. doi: 10.1002/1873-3468.12387. Epub 2016, Sep 18. PMID:27596987<ref>PMID:27596987</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5b4i" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Hagiwara | ==See Also== | ||
[[Category: | *[[Phycocyanobilin:ferredoxin oxidoreductase|Phycocyanobilin:ferredoxin oxidoreductase]] | ||
[[Category: Sugishima | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechocystis sp. PCC 6803]] | |||
[[Category: Fukuyama K]] | |||
[[Category: Hagiwara Y]] | |||
[[Category: Irikawa T]] | |||
[[Category: Sugishima M]] | |||
[[Category: Unno M]] | |||
[[Category: Wada K]] | |||