3QZZ

3D Structure of Ferric Methanosarcina Acetivorans Protoglobin Y61W mutant in Aquomet form

3QZZ の概要

• エントリーDOI: 10.2210/pdb3qzz/pdb
• 関連するPDBエントリー: 2VEB 2VEE 3QZX 3R0G
• 分子名称: Methanosarcina acetivorans protoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: protoglobin, globin fold, methanogenesis, archaea protein, oxygen binding, oxygen transport
• 由来する生物種: Methanosarcina acetivorans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23650.39

構造登録者

Pesce, A.,Tilleman, L.,Dewilde, S.,Ascenzi, P.,Coletta, M.,Ciaccio, C.,Bruno, S.,Moens, L.,Bolognesi, M.,Nardini, M. (登録日: 2011-03-07, 公開日: 2011-06-08, 最終更新日: 2024-02-21)

主引用文献

Pesce, A.,Tilleman, L.,Dewilde, S.,Ascenzi, P.,Coletta, M.,Ciaccio, C.,Bruno, S.,Moens, L.,Bolognesi, M.,Nardini, M.
Structural heterogeneity and ligand gating in ferric methanosarcina acetivorans protoglobin mutants.
Iubmb Life, 63:287-294, 2011

PubMed Abstract: Protoglobin from Methanosarcina acetivorans C2A (MaPgb), a strictly anaerobic methanogenic Archaea, displays peculiar structural and functional properties within members of the hemoglobin superfamily. In fact, MaPgb-specific loops and a N-terminal extension (20 amino acid residues) completely bury the heme within the protein matrix. Therefore, the access of diatomic gaseous molecules to the heme is granted by two apolar tunnels reaching the heme distal site from locations at the B/G and B/E helix interfaces. The presence of two tunnels within the protein matrix could be partly responsible for the slightly biphasic ligand binding behavior. Unusually, MaPgb oxygenation is favored with respect to carbonylation. Here, the crucial role of Tyr(B10)61 and Ile(G11)149 residues, located in the heme distal site and lining the protein matrix tunnels 1 and 2, respectively, on ligand binding to the heme-Fe-atom and on distal site structural organization is reported. In particular, tunnel 1 accessibility is modulated by a complex reorganization of the Trp(B9)60 and Phe(E11)93 side-chains, triggered by mutations of the Tyr(B10)61 and Ile(G11)149 residues, and affected by the presence and type of the distal heme-bound ligand.

PubMed: 21618401
DOI: 10.1002/iub.484

実験手法

X-RAY DIFFRACTION (2.4 Å)