2VEE
Structure of protoglobin from Methanosarcina acetivorans C2A
Summary for 2VEE
Entry DOI | 10.2210/pdb2vee/pdb |
Related | 2VEB |
Descriptor | PROTOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | hemoprotein structure, protein matrix tunnels, protoglobin, methanogenesis, archaea protein, transport protein |
Biological source | METHANOSARCINA ACETIVORANS |
Total number of polymer chains | 8 |
Total formula weight | 189018.80 |
Authors | Nardini, M.,Pesce, A.,Thijs, L.,Saito, J.A.,Dewilde, S.,Alam, M.,Ascenzi, P.,Coletta, M.,Ciaccio, C.,Moens, L.,Bolognesi, M. (deposition date: 2007-10-22, release date: 2008-01-22, Last modification date: 2023-12-13) |
Primary citation | Nardini, M.,Pesce, A.,Thijs, L.,Saito, J.A.,Dewilde, S.,Alam, M.,Ascenzi, P.,Coletta, M.,Ciaccio, C.,Moens, L.,Bolognesi, M. Archaeal Protoglobin Structure Indicates New Ligand Diffusion Paths and Modulation of Haem-Reactivity. Embo Rep., 9:157-, 2008 Cited by PubMed 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 1.3 A 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. PubMed: 18188182DOI: 10.1038/SJ.EMBOR.7401153 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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