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8OMM

Coproporphyrin III - LmCpfC complex soaked 3min with Fe2+

8OMM の概要
エントリーDOI10.2210/pdb8omm/pdb
分子名称Coproporphyrin III ferrochelatase, GLYCEROL, 1,2-ETHANEDIOL, ... (7 entities in total)
機能のキーワードferrochelatase, monomere, heme b, biosynthesis, iron insertion, metal binding protein
由来する生物種Listeria monocytogenes
タンパク質・核酸の鎖数1
化学式量合計36484.08
構造登録者
Gabler, T.,Hofbauer, S. (登録日: 2023-03-31, 公開日: 2023-05-03, 最終更新日: 2023-12-06)
主引用文献Gabler, T.,Dali, A.,Sebastiani, F.,Furtmuller, P.G.,Becucci, M.,Hofbauer, S.,Smulevich, G.
Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.
Protein Sci., 32:e4788-e4788, 2023
Cited by
PubMed Abstract: Understanding the reaction mechanism of enzymes at the molecular level is generally a difficult task, since many parameters affect the turnover. Often, due to high reactivity and formation of transient species or intermediates, detailed information on enzymatic catalysis is obtained by means of model substrates. Whenever possible, it is essential to confirm a reaction mechanism based on substrate analogues or model systems by using the physiological substrates. Here we disclose the ferrous iron incorporation mechanism, in solution, and in crystallo, by the coproporphyrin III-coproporphyrin ferrochelatase complex from the firmicute, pathogen, and antibiotic resistant, Listeria monocytogenes. Coproporphyrin ferrochelatase plays an important physiological role as the metalation represents the penultimate reaction step in the prokaryotic coproporphyrin-dependent heme biosynthetic pathway, yielding coproheme (ferric coproporphyrin III). By following the metal titration with resonance Raman spectroscopy and x-ray crystallography, we prove that upon metalation the saddling distortion becomes predominant both in the crystal and in solution. This is a consequence of the readjustment of hydrogen bond interactions of the propionates with the protein scaffold during the enzymatic catalysis. Once the propionates have established the interactions typical of the coproheme complex, the distortion slowly decreases, to reach the almost planar final product.
PubMed: 37743577
DOI: 10.1002/pro.4788
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.15 Å)
構造検証レポート
Validation report summary of 8omm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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