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Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem‐reactivity

2008; Springer Nature; Volume: 9; Issue: 2 Linguagem: Inglês

10.1038/sj.embor.7401153

1469-3178

Marco Nardini, Alessandra Pesce, Liesbet Thijs, Jennifer A. Saito, Sylvia Dewilde, M. Shahid Alam, Paolo Ascenzi, Massimo Coletta, Chiara Ciaccio, Luc Moëns, Martino Bolognesi,

Neonatal Health and Biochemistry

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 1.3 Å 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.