3ZOM

M.acetivorans protoglobin F145W mutant

3ZOM の概要

• エントリーDOI: 10.2210/pdb3zom/pdb
• 関連するPDBエントリー: 3ZOL
• 分子名称: PROTOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: oxygen transport, haem-distal site mutation, allosteric regulation
• 由来する生物種: METHANOSARCINA ACETIVORANS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47705.12

構造登録者

Tilleman, L.,Abbruzzetti, S.,Ciaccio, C.,De Sanctis, G.,Nardini, M.,Pesce, A.,Desmet, F.,Moens, L.,Van Doorslaer, S.,Bruno, S.,Bolognesi, M.,Ascenzi, P.,Coletta, M.,Viappiani, C.,Dewilde, S. (登録日: 2013-02-22, 公開日: 2014-03-12, 最終更新日: 2023-12-20)

主引用文献

Tilleman, L.,Abbruzzetti, S.,Ciaccio, C.,De Sanctis, G.,Nardini, M.,Pesce, A.,Desmet, F.,Moens, L.,Van Doorslaer, S.,Bruno, S.,Bolognesi, M.,Ascenzi, P.,Coletta, M.,Viappiani, C.,Dewilde, S.
Structural Bases for the Regulation of Co Binding in the Archaeal Protoglobin from Methanosarcina Acetivorans.
Plos One, 10:25959-, 2015

PubMed Abstract: Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb*, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb*. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb*. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb* and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.

PubMed: 26047471
DOI: 10.1371/JOURNAL.PONE.0125959

実験手法

X-RAY DIFFRACTION (2.2 Å)