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Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity (Articolo in rivista)

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Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity (Articolo in rivista) (literal)

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Nardini, M; Pesce, A; Thijs, L; Saito, JA; Dewilde, S; Alam, M; Ascenzi, P; Coletta, M; Ciaccio, C; Moens, L; Bolognesi, M (2008)
Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity
in EMBO reports (Print)
(literal)

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Nardini, M; Pesce, A; Thijs, L; Saito, JA; Dewilde, S; Alam, M; Ascenzi, P; Coletta, M; Ciaccio, C; Moens, L; Bolognesi, M (literal)

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\"[Nardini, Marco; Bolognesi, Martino] Univ Milan, CNR, INFM, Dept Biomol Sci & Biotechnol, I-20133 Milan, Italy; [Coletta, Massimiliano; Ciaccio, Chiara] Univ Roma Tor Vergata, Dept Expt Med & Biochem Sci, I-00133 Rome, Italy; [Pesce, Alessandra] Univ Genoa, Dept Phys, CNR, INFM, I-16146 Genoa, Italy; [Pesce, Alessandra] Univ Genoa, CEBR, I-16146 Genoa, Italy; [Thijs, Liesbet; Dewilde, Sylvia; Moens, Luc] Univ Antwerp, Dept Biomed Sci, B-2610 Antwerp, Belgium; [Saito, Jennifer A.; Alam, Maqsudul] Univ Hawaii, Dept Microbiol, Honolulu, HI 96822 USA; [Ascenzi, Paolo] Univ Roma Tre, Dept Biol, I-00146 Rome, Italy; [Ascenzi, Paolo] Univ Roma Tre, Interdept Laab Electron Microscopy, I-00146 Rome, Italy (literal)

Titolo

Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity (literal)

Abstract

The structural adaptability of the globin fold has been highlighted by the recent discovery of the 2-on-2 haemoglobins, of neuroglobin and cytoglobin. Protoglobin from Methanosarcina acetivorans C2A - a strictly anaerobic methanogenic Archaea - is, to the best of our knowledge, the latest entry adding new variability and functional complexity to the haemoglobin (Hb) superfamily. Here, we report the 11.3 angstrom crystal structure of oxygenated M. acetivorans protoglobin, together with the first insight into its ligand-binding properties. We show that, contrary to all known globins, protoglobin-specific loops and an amino-terminal extension completely bury the haem within the protein matrix. Access of O-2, CO and NO to the haem is granted by the protoglobin-specific apolar tunnels reaching the haem distal site from locations at the B/G and B/E helix interfaces. Functionally, M. acetivorans dimeric protoglobin shows a selectivity ratio for O-2/CO binding to the haem that favours O-2 ligation and anticooperativity in ligand binding. Both properties are exceptional within the Hb superfamily. (literal)

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