Phycocyanobilin:ferredoxin oxidoreductase

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== Structural highlights ==
== Structural highlights ==
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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>.
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The U-shaped porphyrin-like substrate of PcyA - <scene name='47/478503/Cv/2'>biliverdin IX-α - binds between the central β sheets and the C terminal α helices</scene><ref>PMID:20946883</ref>.
</StructureSection>
</StructureSection>
== 3D Structures of Phycocyanobilin:ferredoxin oxidoreductase==
== 3D Structures of Phycocyanobilin:ferredoxin oxidoreductase==

Revision as of 12:25, 10 August 2016

Phycocyanobilin:ferredoxin oxidoreductase complex with biliverdin IX-α (PDB entry 3ajg)

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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

  1. ↑ 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
  2. ↑ 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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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