3ajh

<StructureSection load='3ajh' size='340' side='right' caption='[[3ajh]], [[Resolution|resolution]] 2.25&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ajh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis Synechocystis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AJH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BL3:3-[2-[(Z)-[3-(2-CARBOXYETHYL)-5-[(Z)-(3-ETHENYL-4-METHYL-5-OXO-PYRROL-2-YLIDENE)METHYL]-4-METHYL-PYRROL-2-YLIDENE]METHYL]-5-[(Z)-(3-ETHENYL-4-METHYL-5-OXO-PYRROL-2-YLIDENE)METHYL]-4-METHYL-1H-PYRROL-3-YL]PROPANOIC+ACID'>BL3</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase Phycocyanobilin:ferredoxin oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.5 1.3.7.5] </span></td></tr>

<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=3ajh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ajh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ajh RCSB], [http://www.ebi.ac.uk/pdbsum/3ajh PDBsum]</span></td></tr>

== 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>

 

== References ==

<references/>

[[Category: Phycocyanobilin:ferredoxin oxidoreductase]]

[[Category: Synechocystis]]

[[Category: Fukuyama, K.]]

[[Category: Hagiwara, Y.]]

[[Category: Wada, K.]]

[[Category: Oxidoreductase]]