8BBV

Coproporphyrin III - LmCpfC complex soaked 2min with Fe2+

8BBV の概要

• エントリーDOI: 10.2210/pdb8bbv/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 activity metal ion binding heme b biosynthesis, 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: 36594.31

構造登録者

Gabler, T.,Hofbauer, S. (登録日: 2022-10-14, 公開日: 2023-01-11, 最終更新日: 2024-02-07)

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

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

実験手法

X-RAY DIFFRACTION (2.19 Å)