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.

@article{Coppola2012ATPRO,
  title={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.},
  author={Daniela Coppola and Stefania Abbruzzetti and Francesco P. Nicoletti and Antonello Merlino and Alessandra Gambacurta and Daniela Giordano and Barry D. Howes and Giampiero de Sanctis and Luigi Vitagliano and Stefano Bruno and Guido di Prisco and Lelio Mazzarella and Giulietta Smulevich and Massimo Coletta and Cristiano Viappiani and Alessandro Vergara and Cinzia Verde},
  journal={Molecular bioSystems},
  year={2012},
  volume={8 12},
  pages={
          3295-304
        }
}
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… 
View on PubMed
rsc.org
11 Citations
Highly Influential Citations
1
Background Citations
5
Methods Citations
3
Results Citations
2

Figures from this paper

11 Citations

Citation Type

Citation Type

Functional characterisation of the haemoglobins of the migratory notothenioid fish Dissostichus eleginoides
TLDR
The amino-acid sequence reveals high identity with the globins of Antarctic notothenioids, arguing in favour of a common origin within nototenioid, and indicates that the primary structure of the major and minor haemoglobins has undergone modifications only to a limited extent.
The unique structural features of carbonmonoxy hemoglobin from the sub-Antarctic fish Eleginops maclovinus
TLDR
The crystal structure of a carbonmonoxy form of the Hb isolated from the sub-Antarctic notothenioid fish Eleginops maclovinus characterised by either rare or unique features is reported, providing a rationale for some spectroscopic properties exhibited by the protein in solution.
Crystal structure of monocarboxylated hemoglobin from the sub-Antarctic fish Eleginops maclovinus
TLDR
The crystal structure of a carbonmonoxy form of the Hb isolated from the sub-Antarctic notothenioid fish Eleginops maclovinus characterised by either rare or unique features is reported, providing a rationale for some spectroscopic properties exhibited by the protein in solution.
Role of tertiary structures on the Root effect in fish hemoglobins.
The Greenland shark Somniosus microcephalus—Hemoglobins and ligand-binding properties
TLDR
The very similar ligand-binding properties of the hemoglobins of the Arctic shark Somniosus microcephalus suggest that regulatory control of O2 transport may be at the cellular level and that it may involve changes in the cellular concentrations of allosteric effectors and/or variations of other systemic factors.
Fine Sampling of the R→T Quaternary-Structure Transition of a Tetrameric Hemoglobin.
TLDR
The X-ray structures of two independent tetramers of the fully ligated carbomonoxy form of Trematomus newnesi hemoglobin within the same crystal are described, providing the best available atomic-level picture of the R→T transition of vertebrate Hbs.
Adaptations to environmental change: Globin superfamily evolution in Antarctic fishes.
The Ross Sea and its rich life: research on molecular adaptive evolution of stenothermal and eurythermal Antarctic organisms and the Italian contribution
TLDR
An overview of the wide-ranging research in marine biology performed in the last three decades by the author’s team in the Ross Sea is presented.
Antarctic ecosystems in transition – life between stresses and opportunities
  • J. Gutt, E. Isla, +22 authors D. Wall
  • Environmental Science
    Biological reviews of the Cambridge Philosophical Society
  • 2020
Important findings from the second decade of the 21st century on the impact of environmental change on biological processes in the Antarctic were synthesised by 26 international experts. Ten key…
Using cryo-electron microscopy maps for X-ray structure determination of homologues.
TLDR
This hybrid method consistently produced models with reasonable Rwork and Rfree values which agree well with the previously determined X-ray structures for all test cases, indicating the general applicability of the method for X-rays structure determination of homologues using cryo-EM maps as a starting point.
...
1
2
...

References

SHOWING 1-10 OF 38 REFERENCES
Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative.
The hemoglobins of the sub‐Antarctic fish Cottoperca gobio, a phyletically basal species – oxygen‐binding equilibria, kinetics and molecular dynamics
TLDR
The structure, function and evolution of the oxygen‐transport system of Cottoperca gobio, a sub‐Antarctic notothenioid fish of the family Bovichtidae, probably derived from ancestral species that evolved in the Antarctic region and later migrated to lower latitudes is focused on.
Structural-functional characterization of the cathodic haemoglobin of the conger eel Conger conger: molecular modelling study of an additional phosphate-binding site.
TLDR
A computer modelling study has been performed on the basis of the amino acid sequence of the alpha- and beta-chains, which suggest that C. conger cathodic Hb may bind organic phosphates at two distinct binding sites located along the central cavity of the tetramer by hydrogen bonds and/or electrostatic interactions with amino acid residues of both chains, which have been identified.
High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect
TLDR
The high‐resolution structure of the deoxy form of Hb isolated from the Antarctic fish Trematomus bernacchii crystallized at pH 6.2 and 8.4 sheds light on the role played by the histidine residues in modulating the strength of the Root effect and support the emerging idea that the structural determinants are specific of each Hb endowed with this property.
Crystal structure of Trematomus newnesi haemoglobin re-opens the root effect question.
TLDR
The structure of Trematomus newnesi Hb 1 is similar to that of Root effect fish Hbs from Spot and T. bernacchii, suggesting that the differences in the pH dependence cannot be related to the modulation of the R-state.
Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes
TLDR
Molecular modeling, electronic absorption and resonance Raman spectra have been used to characterize the heme environment of Hb 1 in an attempt to explain these features, particularly in view of some potentially important nonconservative replacements found in the primary structure.
The hemoglobins of sub-Antarctic fishes of the suborder Notothenioidei
Structural characterization of ferric hemoglobins from three antarctic fish species of the suborder notothenioidei.
TLDR
Structural characterization by EPR of the oxidized states of tetrameric Hbs isolated from the Antarctic fish species Trematomus bernacchii, Trem atomus newnesi, and Gymnodraco acuticeps is reported, showing that ferric states commonly associated with monomeric and dimeric Hbs are also found in tetramerIC Hbs.
Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study.
Antarctic fish hemoglobin: an outline of the molecular structure and oxygen binding properties—I. Molecular structure
...
1
2
3
4
...