1C1H

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FERROCHELATASE IN COMPLEX WITH N-METHYL MESOPORPHYRIN

1C1H の概要

• エントリーDOI: 10.2210/pdb1c1h/pdb
• 関連するPDBエントリー: 1AK1
• 分子名称: FERROCHELATASE, MAGNESIUM ION, N-METHYLMESOPORPHYRIN, ... (4 entities in total)
• 機能のキーワード: rossmann fold, alpha/beta fold, ferrochelatase, heme synthesis, porphyrin metallation, pi-helix, lyase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: P32396
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35994.73

構造登録者

Lecerof, D.,Fodje, M.,Hansson, A.,Hansson, M.,Al-Karadaghi, S. (登録日: 1999-07-22, 公開日: 2000-03-17, 最終更新日: 2024-03-13)

主引用文献

Lecerof, D.,Fodje, M.,Hansson, A.,Hansson, M.,Al-Karadaghi, S.
Structural and mechanistic basis of porphyrin metallation by ferrochelatase.
J.Mol.Biol., 297:221-232, 2000

PubMed Abstract: Ferrochelatase, the enzyme catalyzing metallation of protoporphyrin IX at the terminal step of heme biosynthesis, was co-crystallized with an isomer mixture of the potent inhibitor N-methylmesoporphyrin (N-MeMP). The X-ray structure revealed the active site of the enzyme, to which only one of the isomers was bound, and for the first time allowed characterization of the mode of porphyrin macrocycle distortion by ferrochelatase. Crystallization of ferrochelatase and N-MeMP in the presence of Cu(2+) leads to metallation and demethylation of N-MeMP. A mechanism of porphyrin distortion is proposed, which assumes that the enzyme holds pyrrole rings B, C and D in a vice-like grip and forces a 36 degrees tilt on ring A.

PubMed: 10704318
DOI: 10.1006/jmbi.2000.3569

実験手法

X-RAY DIFFRACTION (1.9 Å)