5B3V

Crystal structure of biliverdin reductase in complex with biliverdin and NADP+ from Synechocystis sp. PCC 6803

5B3V の概要

• エントリーDOI: 10.2210/pdb5b3v/pdb
• 関連するPDBエントリー: 5B3T 5B3U
• 分子名称: Biliverdin reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, BILIVERDINE IX ALPHA, ... (4 entities in total)
• 機能のキーワード: biliverdin reductase, heme degrading pathway, nad(p)h-dependent enzyme, tetrapyrrole, rossmann fold, transferase
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155489.87

構造登録者

Takao, H.,Wada, K. (登録日: 2016-03-13, 公開日: 2017-02-15, 最終更新日: 2023-11-08)

主引用文献

Takao, H.,Hirabayashi, K.,Nishigaya, Y.,Kouriki, H.,Nakaniwa, T.,Hagiwara, Y.,Harada, J.,Sato, H.,Yamazaki, T.,Sakakibara, Y.,Suiko, M.,Asada, Y.,Takahashi, Y.,Yamamoto, K.,Fukuyama, K.,Sugishima, M.,Wada, K.
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity
Nat Commun, 8:14397-14397, 2017

PubMed Abstract: Biliverdin reductase catalyses the last step in haem degradation and produces the major lipophilic antioxidant bilirubin via reduction of biliverdin, using NAD(P)H as a cofactor. Despite the importance of biliverdin reductase in maintaining the redox balance, the molecular details of the reaction it catalyses remain unknown. Here we present the crystal structure of biliverdin reductase in complex with biliverdin and NADP. Unexpectedly, two biliverdin molecules, which we designated the proximal and distal biliverdins, bind with stacked geometry in the active site. The nicotinamide ring of the NADP is located close to the reaction site on the proximal biliverdin, supporting that the hydride directly attacks this position of the proximal biliverdin. The results of mutagenesis studies suggest that a conserved Arg185 is essential for the catalysis. The distal biliverdin probably acts as a conduit to deliver the proton from Arg185 to the proximal biliverdin, thus yielding bilirubin.

PubMed: 28169272
DOI: 10.1038/ncomms14397

実験手法

X-RAY DIFFRACTION (2.594 Å)