2G18
Crystal Structure of Nostoc sp. 7120 phycocyanobilin:ferredoxin oxidoreductase (PcyA) Apoprotein
2G18 の概要
| エントリーDOI | 10.2210/pdb2g18/pdb |
| 分子名称 | Phycocyanobilin:ferredoxin oxidoreductase, CALCIUM ION (3 entities in total) |
| 機能のキーワード | alpha-beta-alpha sandwich, oxidoreductase |
| 由来する生物種 | Anabaena sp. |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 345107.65 |
| 構造登録者 | |
| 主引用文献 | Tu, S.L.,Rockwell, N.C.,Lagarias, J.C.,Fisher, A.J. Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements. Biochemistry, 46:1484-1494, 2007 Cited by PubMed Abstract: The X-ray crystal structure of the substrate-free form of phycocyanobilin (PCB)-ferredoxin oxidoreductase (PcyA; EC 1.3.7.5) from the cyanobacterium Nostoc sp. PCC7120 has been solved at 2.5 A resolution. A comparative analysis of this structure with those recently reported for substrate-bound and substrate-free forms of PcyA from the cyanobacterium Synechocystis sp. PCC6803 (Hagiwara et al. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 27-32; Hagiwara et al. (2006) FEBS Lett. 580, 3823-3828) provides a compelling picture of substrate-induced changes in the PcyA enzyme and the chemical basis of PcyA's catalytic activity. On the basis of these structures and the biochemical analysis of site-directed mutants of Nostoc PcyA, including mutants reported in recent studies (Tu et al. (2006) J. Biol. Chem. 281, 3127-3136) as well as mutants described in this study, a revised mechanism for the PcyA-mediated four-electron reduction of biliverdin IXalpha to 3E/3Z-phycocyanobilin via enzyme-bound bilin radical intermediates is proposed. The mechanistic insight of these studies, along with homology modeling, have provided new insight into the catalytic mechanisms of other members of the ferredoxin-dependent bilin reductase family that are widespread in oxygenic photosynthetic organisms. PubMed: 17279614DOI: 10.1021/bi062038f 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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