Affiliations: Dipto. Chim. Dell'Univ. Napoli F., Via Mezzocannone, 4, I-80134, Napoli, Italy
Ist. Biochim. Delle Proteine Ed E., CNR, Via Marconi 10, I-80125, Napoli, Italy
Department of Biochemistry, University of Leicester, Leicester, LE1 7RH, United Kingdom
References: Baldwin, J.M., Chothia, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) J. Mol. Biol., 129, pp. 175-22
Brünger, A.T., (1992) X-PLOR Manual, Version 3.1, , New Haven: Yale University Press
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 (1992) J. Mol. Biol., 224, pp. 449-460
D'Avino, R., Caruso, C., Tamburrini, M., Romano, M., Rutigliano, B., Polverino De Laureto, P., Camardella, L., Di Prisco, G., Molecular characterization of the functionally distinct haemoglobins of the Antarctic fish Trematomus newnesi (1994) J. Biol. Chem., 269, pp. 9675-9681
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 (1990) J. Mol. Biol., 211, pp. 515-519
Di Prisco, G., Physiological and biochemical adaptations in fish to a cold marine environment (1997) Antarctic Communities, Species, Structure and Survival, pp. 251-260. , B. Battaglia, J. Valencia, & D. W. H. Walton. Cambridge: Cambridge University Press
Di Prisco, G., Tamburrini, M., D'Avino, R., Oxygen transport systems in extreme environments: Multiplicity and structure/function relationships in haemoglobin of Antarctic fish (1997) Cold Ocean Physiology, pp. 143-165. , H. O. Pörtner, & R. C. Playle. Cambridge: Cambridge University Press
Hendrikson, W.A., Stereochemically restrained refinement of macromolecular structures (1985) Methods Enzymol., 115, pp. 252-270
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 (1995) J. Mol. Biol., 250, pp. 648-658
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 (1991) Acta Crystallog. Sect. a, 47, pp. 110-119
Kraulis, P.J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallog., 24, pp. 946-950
Laskowskoi, R.A., MacArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A program to check for stereochemical quality of protein structures (1993) J. Appl. Crystallog., 26, pp. 283-291
Leslie, A.G.W., Recent changes to the MOSFLM package for processing film and image plate data (1992) CCP4 and ESF-EACMB Newsletter on Protein Crystallography No.26, , Warrington: SERCDaresbury Laboratory
Merrit, E., Murphy, M., RASTER3D version 2.0: A program for photorealistic molecular graphics (1994) Acta Crystallog. Sect. D, 50, pp. 869-879
Mylvaganam, S.E., Bonaventura, C., Bonaventura, J., Getzoff, E.D., Structural basis for the Root effect in haemoglobin (1996) Nature Struct. Biol., 3, pp. 275-283
Perutz, M.F., Cause of the Root effect in fish haemoglobin (1996) Nature Struct. Biol., 3, pp. 211-212
Perutz, M.F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian haemoglobins (1982) Nature, 299, pp. 421-426
Perutz, M.F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R., Stereochemistry of cooperative mechanism in hemoglobin (1987) Acc. Chem. Res., 20, pp. 309-321
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 (1993) J. Mol. Biol., 230, pp. 1291-1296
Tame, J.R.H., Wilson, J.C., Weber, R.E., The crystal structures of Trout Hb I in the deoxy and carbonmonoxy forms (1996) J. Mol. Biol., 259, pp. 749-760
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 (1993) J. Appl. Physiol., 75, pp. 2646-2655
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 (1996) J. Mol. Biol., 255, pp. 484-493
Baldwin, J. M., Chothia, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) J. Mol. Biol., 129, pp. 175-22
Br nger, A. T., (1992) X-PLOR Manual, Version 3. 1, , New Haven: Yale University Press
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 (1990) J. Mol. Biol., 211, pp. 515-519
Hendrikson, W. A., Stereochemically restrained refinement of macromolecular structures (1985) Methods Enzymol., 115, pp. 252-270
Jones, T. A., Interactive computer graphics: FRODO (1985) Methods. Enzymol., 115, pp. 157-171
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 (1991) Acta Crystallog. Sect. a, 47, pp. 110-119
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallog., 24, pp. 946-950
Laskowskoi, R. A., MacArthur, M. W., Moss, D. S., Thornton, J. M., PROCHECK: A program to check for stereochemical quality of protein structures (1993) J. Appl. Crystallog., 26, pp. 283-291
Leslie, A. G. W., Recent changes to the MOSFLM package for processing film and image plate data (1992) CCP4 and ESF-EACMB Newsletter on Protein Crystallography No. 26, , Warrington: SERCDaresbury Laboratory
Mylvaganam, S. E., Bonaventura, C., Bonaventura, J., Getzoff, E. D., Structural basis for the Root effect in haemoglobin (1996) Nature Struct. Biol., 3, pp. 275-283
Perutz, M. F., Cause of the Root effect in fish haemoglobin (1996) Nature Struct. Biol., 3, pp. 211-212
Perutz, M. F., Brunori, M., Stereochemistry of cooperative effects in fish and amphibian haemoglobins (1982) Nature, 299, pp. 421-426
Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R., Stereochemistry of cooperative mechanism in hemoglobin (1987) Acc. Chem. Res., 20, pp. 309-321
Shih, D. T., Luisi, B. F., Miyazaky, G., Perutz, M. F., Nagai, K., A mutagenic study of the allosteric linkage of His (HC3) 146 in haemoglobin (1993) J. Mol. Biol., 230, pp. 1291-1296
Tame, J. R. H., Wilson, J. C., Weber, R. E., The crystal structures of Trout Hb I in the deoxy and carbonmonoxy forms (1996) J. Mol. Biol., 259, pp. 749-760
Weber, R. E., Jessen, T. -H., Malte, H., Tame, J., Mutant hemoglobins (119-Ala and 55-Ser): Functions related to high altitude respiration in geese (1993) J. Appl. Physiol., 75, pp. 2646-2655
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question
As new structural data have become available, somewhat contrasting explanations of the Root effect in fish haemoglobins (Hb) have been provided. Hb 1 of the Antarctic fish Trematomus newnesi has a nearly pH-independent oxygen affinity, in spite of 95 % sequence identity with Hb 1 of Trematomus (previously named Pagothenia) bernacchii that has a strong Root effect. Here, the 2.2 Angstrom R-state structure of Trematomus newnesi Ho 1 is presented. The structure is similar to that of Root effect fish Kbs from Spot and T. bernacchii, suggesting that the differences in the pH dependence cannot be related to the modulation of the R-state. In comparison to T, bernacchii Hb 1, the role of the three mutations Thr41 (C6)alpha --> Ile, Ala97 (G3)alpha --> Ser and His41 (C7)beta --> Tyr at the alpha(1)beta(2)-interface is discussed. (C) 1999 Academic Press.
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question