View source for 3ajg


==Crystal structure of PcyA V225D-biliverdin IX alpha complex==
<StructureSection load='3ajg' size='340' side='right'caption='[[3ajg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ajg]] is a 2 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=3AJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AJG 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]] 1.9&#8491;</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=3ajg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ajg OCA], [https://pdbe.org/3ajg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ajg RCSB], [https://www.ebi.ac.uk/pdbsum/3ajg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ajg 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 sequential reduction of the vinyl group of the D-ring and A-ring of biliverdin IXalpha (BV), using reducing equivalents provided by ferredoxin. This reaction produces phycocyanobilin, a pigment used for light-harvesting and light-sensing in red algae and cyanobacteria. The crystal structure of PcyA-BV reveals that BV is specifically bound in the PcyA active pocket through extensive hydrophobic and hydrophilic interactions. During the course of a mutational study of PcyA, we observed that mutation of the V225 position, apart from the processing sites, conferred an unusual property on PcyA; V225D mutant protein could bind BV and its analog BV13, but these complexes showed a distinct UV-vis absorption spectrum from that of the wild-type PcyA-BV complex. The crystal structures of BV- and BV13-bound forms of V225D protein revealed that gross structural changes occurred near the substrate-binding pocket, and that the BV/BV13 binding manner in the pocket was dramatically altered. Protein folding in V225D-BV/BV13 was more similar to that of substrate-free PcyA than that in PcyA-BV; the "induced-fit" did not occur when BV/BV13 was bound to the V225D protein. The unexpected structural change presented here provides a cautionary note about interpreting functional data derived from a mutated protein in the absence of its exact structure.

One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding.,Wada K, Hagiwara Y, Yutani Y, Fukuyama K Biochem Biophys Res Commun. 2010 Nov 12;402(2):373-7. Epub 2010 Oct 12. PMID:20946883<ref>PMID:20946883</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ajg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phycocyanobilin:ferredoxin oxidoreductase|Phycocyanobilin:ferredoxin oxidoreductase]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Fukuyama K]]
[[Category: Hagiwara Y]]
[[Category: Wada K]]