Phycocyanobilin:ferredoxin oxidoreductase
From Proteopedia
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| - | <StructureSection load='3ajg' size=' | + | <StructureSection load='3ajg' size='450' side='right' caption='Phycocyanobilin:ferredoxin oxidoreductase complex with biliverdin IX-α (PDB entry [[3ajg]])' scene='47/478503/Cv/1'> |
== Function == | == Function == | ||
'''Phycocyanobilin:ferredoxin oxidoreductase''' (PcyA) is a member of the Fd-dependent bilin family. PcyA reduces vinyl groups of biliverdin IX-α to yield phycocyanobilin<ref>PMID:15250720</ref>. Phycocyanobilin is a pigment precursor of the light-harvesting antennae in red algae and cyanobacteria. | '''Phycocyanobilin:ferredoxin oxidoreductase''' (PcyA) is a member of the Fd-dependent bilin family. PcyA reduces vinyl groups of biliverdin IX-α to yield phycocyanobilin<ref>PMID:15250720</ref>. Phycocyanobilin is a pigment precursor of the light-harvesting antennae in red algae and cyanobacteria. | ||
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== Structural highlights == | == Structural highlights == | ||
The U-shaped porphyrin-like substrate of PcyA - biliverdin IX-α - binds between the central β sheets and the C terminal α helices<ref>PMID:20946883</ref>. | The U-shaped porphyrin-like substrate of PcyA - biliverdin IX-α - binds between the central β sheets and the C terminal α helices<ref>PMID:20946883</ref>. | ||
| + | </StructureSection> | ||
== 3D Structures of Phycocyanobilin:ferredoxin oxidoreductase== | == 3D Structures of Phycocyanobilin:ferredoxin oxidoreductase== | ||
Revision as of 12:20, 10 August 2016
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3D Structures of Phycocyanobilin:ferredoxin oxidoreductase
3ajg, 3i95 – SyPcyA (mutant) + biliverdin IX – Synechocystis
3ajh – SyPcyA (mutant) + biliverdin XIII
3i94 - SyPcyA + biliverdin XIII
3f0l, 3fom, 3nb8, 3nb9 – SyPcyA (mutant)
3i8u – SyPcyA + biliverdin derivative
References
- ↑ Tu SL, Gunn A, Toney MD, Britt RD, Lagarias JC. Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates. J Am Chem Soc. 2004 Jul 21;126(28):8682-93. PMID:15250720 doi:http://dx.doi.org/10.1021/ja049280z
- ↑ Wada K, Hagiwara Y, Yutani Y, Fukuyama K. One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding. Biochem Biophys Res Commun. 2010 Nov 12;402(2):373-7. Epub 2010 Oct 12. PMID:20946883 doi:10.1016/j.bbrc.2010.10.037
