4ESA

X-ray structure of carbonmonoxy hemoglobin of Eleginops maclovinus

Summary for 4ESA

• Entry DOI: 10.2210/pdb4esa/pdb
• Related: 1PBX 1T1N 2AA1 2H8D 2H8F 3gkv
• Descriptor: Hemoglobin alpha chain, Hemoglobin beta chain, CARBON MONOXIDE, ... (6 entities in total)
• Functional Keywords: haemoglobin, ligand-binding properties, root effect, quaternary structure, structure/function relationship, oxygen transporter, o2, blood, oxygen transport
• Biological source: Eleginops maclovinus; More
• Total number of polymer chains: 4
• Total formula weight: 66349.48

Authors

Merlino, A.,Vitagliano, L.,Mazzarella, L.,Vergara, A. (deposition date: 2012-04-23, release date: 2012-11-07, Last modification date: 2024-10-30)

Primary citation

Coppola, D.,Abbruzzetti, S.,Nicoletti, F.,Merlino, A.,Gambacurta, A.,Giordano, D.,Howes, B.D.,De Sanctis, G.,Vitagliano, L.,Bruno, S.,di Prisco, G.,Mazzarella, L.,Smulevich, G.,Coletta, M.,Viappiani, C.,Vergara, A.,Verde, C.
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus.
Mol Biosyst, 8:3295-3304, 2012

PubMed Abstract: The major haemoglobin of the sub-Antarctic fish Eleginops maclovinus was structurally and functionally characterised with the aim to compare molecular environmental adaptations in the O(2)-transport system of sub-Antarctic fishes of the suborder Notothenioidei with those of their high-latitude relatives. Ligand-binding kinetics of the major haemoglobin of E. maclovinus indicated strong stabilisation of the liganded quaternary T state, enhanced in the presence of the physiological allosteric effector ATP, compared to that of high-Antarctic Trematomus bernacchii. The activation enthalpy for O(2) dissociation was dramatically lower than that in T. bernacchii haemoglobin, suggesting remarkable differences in temperature sensitivity and structural changes associated with O(2) release and exit from the protein. The haemoglobin functional properties, together with the X-ray structure of the CO form at 1.49 Å resolution, the first of a temperate notothenioid, strongly support the hypothesis that in E. maclovinus, whose life-style varies according to changes in habitat, the mechanisms that regulate O(2) affinity and the ATP-induced Root effect differ from those of high-Antarctic Notothenioids.

PubMed: 23086282
DOI: 10.1039/c2mb25210d

Experimental method

X-RAY DIFFRACTION (1.45 Å)