Crystal structure of trematomus newnesi haemoglobin re-opens the root effect question

Journal of Molecular Biology

Volumn 287, Issue 5, 1999, Pages 897-906

  Mazzarella, Lelio ^a   D'Avino, Rossana ^b   Di Prisco, Guido ^b   Savino, Carmelinda ^a   Vitagliano, Luigi ^a   Moody, Peter C E ^c   Zagari, Adriana ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

Antarctic fish; Haemoglobin; Root effect; Trematomus newnesi; X ray structure

Indexed keywords

HEMOGLOBIN; MUTANT PROTEIN; OXYGEN;

ARTICLE; CRYSTAL STRUCTURE; FISH; NONHUMAN; OXYGEN AFFINITY; PH; PRIORITY JOURNAL; SEQUENCE HOMOLOGY;

EID: 0033574669     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2632     Document Type: Article

References (23)

1. Baldwin J. M., Chothia C. Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129:1979;175-220.
2. Brünger A. T. X-PLOR Manual, Version 3.1. 1992;Yale University Press, New Haven.
3. Camardella L., Caruso C., D'Avino R., di Prisco G., Rutigliano B., Tamburrini M., Fermi G., Perutz M. F. Haemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J. Mol. Biol. 224:1992;449-460.
4. D'Avino R., Caruso C., Tamburrini M., Romano M., Rutigliano B., Polverino de Laureto P., Camardella L., Carratore V., di Prisco G. Molecular characterization of the functionally distinct haemoglobins of the Antarctic fish Trematomus newnesi. J. Biol. Chem. 269:1994;9675-9681.
5. Derewenda Z. D., Dodson G. G., Emsley P., Harris D., Nagai K., Perutz M. F., Reynard J.-P. Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobin. J. Mol. Biol. 211:1990;515-519.
6. di Prisco G. Physiological and biochemical adaptations in fish to a cold marine environment. Battaglia B., Valencia J., Walton D. W. H. Antarctic Communities, Species, Structure and Survival. 1997;251-260 Cambridge University Press, Cambridge.
7. di Prisco G., Tamburrini M., D'Avino R. Oxygen transport systems in extreme environments: multiplicity and structure/function relationships in haemoglobin of Antarctic fish. Pörtner H. O., Playle R. C. Cold Ocean Physiology. 1997;143-165 Cambridge University Press, Cambridge.
8. Hendrikson W. A. Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115:1985;252-270.
9. Ito N., Komiyama N. H., Fermi G. Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded haemoglobin structures. J. Mol. Biol. 250:1995;648-658.
10. Jones T. A. Interactive computer graphics: FRODO. Methods. Enzymol. 115:1985;157-171.
11. Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
12. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
13. Laskowskoi R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check for stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
14. Leslie A. G. W. Recent changes to the MOSFLM package for processing film and image plate data. CCP4 and ESF-EACMB Newsletter on Protein Crystallography No.26. 1992;SERCDaresbury Laboratory, Warrington.
15. Merrit E., Murphy M. RASTER3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-879.
16. Mylvaganam S. E., Bonaventura C., Bonaventura J., Getzoff E. D. Structural basis for the Root effect in haemoglobin. Nature Struct. Biol. 3:1996;275-283.
17. Perutz M. F. Cause of the Root effect in fish haemoglobin. Nature Struct. Biol. 3:1996;211-212.
18. Perutz M. F., Brunori M. Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature. 299:1982;421-426.
19. Perutz M. F., Fermi G., Luisi B., Shaanan B., Liddington R. Stereochemistry of cooperative mechanism in hemoglobin. Acc. Chem. Res. 20:1987;309-321.
20. Shih D. T., Luisi B. F., Miyazaky G., Perutz M. F., Nagai K. A mutagenic study of the allosteric linkage of His(HC3)146 β in haemoglobin. J. Mol. Biol. 230:1993;1291-1296.
21. Tame J. R. H., Wilson J. C., Weber R. E. The crystal structures of Trout Hb I in the deoxy and carbonmonoxy forms. J. Mol. Biol. 259:1996;749-760.
22. Weber R. E., Jessen T.-H., Malte H., Tame J. Mutant hemoglobins (α119-Ala and β55-Ser): functions related to high altitude respiration in geese. J. Appl. Physiol. 75:1993;2646-2655.
23. Zhang J., Hua Z., Tame J. R. H., Zhang G. L. R., Gu X. The crystal structure of a high oxygen affinity species of haemoglobin. J. Mol. Biol. 255:1996;484-493.