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2VEE

Structure of protoglobin from Methanosarcina acetivorans C2A

Summary for 2VEE
Entry DOI10.2210/pdb2vee/pdb
Related2VEB
DescriptorPROTOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordshemoprotein structure, protein matrix tunnels, protoglobin, methanogenesis, archaea protein, transport protein
Biological sourceMETHANOSARCINA ACETIVORANS
Total number of polymer chains8
Total formula weight189018.80
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 citationNardini, 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: 18188182
DOI: 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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