3X16

Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942

3X16 の概要

• エントリーDOI: 10.2210/pdb3x16/pdb
• 関連するPDBエントリー: 3WNU
• 分子名称: Catalase-peroxidase, HEME B/C, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: peroxidase, catalase subfamily, oxidoreductase, heme b fe, cross-link, trp-tyr-met adduct
• 由来する生物種: Synechococcus elongatus PCC 7942
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 80815.10

構造登録者

Tada, T.,Wada, K.,Kamachi, S. (登録日: 2014-10-30, 公開日: 2014-12-24, 最終更新日: 2024-05-29)

主引用文献

Kamachi, S.,Hirabayashi, K.,Tamoi, M.,Shigeoka, S.,Tada, T.,Wada, K.
Crystal structure of the catalase-peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro-drug isoniazid.
Febs Lett., 589:131-137, 2015

PubMed Abstract: Isoniazid (INH) is a pro-drug that has been extensively used to treat tuberculosis. INH is activated by the heme enzyme catalase-peroxidase (KatG), but the mechanism of the activation is poorly understood, in part because the INH binding site has not been clearly established. Here, we observed that a single-residue mutation of KatG from Synechococcus elongatus PCC7942 (SeKatG), W78F, enhances INH activation. The crystal structure of INH-bound KatG-W78F revealed that INH binds to the heme pocket. The results of a thermal-shift assay implied that the flexibility of the SeKatG molecule is increased by the W78F mutation, allowing the INH molecule to easily invade the heme pocket through the access channel on the γ-edge side of the heme.

PubMed: 25479089
DOI: 10.1016/j.febslet.2014.11.037

実験手法

X-RAY DIFFRACTION (2.65 Å)