The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)

Journal of Molecular Biology

Volumn 255, Issue 3, 1996, Pages 484-493

  Zhang, Jian ^a,c   Hua, Ziqian ^a   Tame, Jeremy R H ^b   Lu, Guangying ^a   Zhang, Renji ^a   Gu, Xiaocheng ^a  

^a PEKING UNIVERSITY   (China)

^b UNIVERSITY OF YORK   (United Kingdom)

^c INSTITUTE OF BIOPHYSICS   (China)

Author keywords

Crystallography; Haemoglobin; High altitude adaptation

Indexed keywords

ALANINE; HEMOGLOBIN; HEMOGLOBIN A; INOSITOL PENTAKISPHOSPHATE; OXYHEMOGLOBIN; PROLINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; BLOOD; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; GOOSE; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; R FACTOR;

EID: 0029912404     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0040     Document Type: Article

References (39)

1. 1 interface in hemoglobin completely destabilizes the T state. J. Biol. Chem. 264, 17745-17749.
2. Arnone, A. (1972). X-ray diffraction study of binding of 2,3 diphosphoglycerate to human haemoglobin. Nature, 237, 146-149.
3. Baldwin, J. & Chothia, C. (1979). Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129, 175-220.
4. Brunger, A. T. (1992). XPLOR version 3.1, Yale University, CT, USA.
5. Camardella, L., Caruso, C., D'Avino, R., di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G. & Perutz, M. F. (1992). Haemoglobin of the Antarctic fish Pagothenia bernachii: amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative. J. Mol. Biol. 224, 449-460.
6. (1994). The CCP4 Suite: programs for protein crystallography. Acta Crystallog. sect D, 50, 760-763.
7. Demma, L. S. & Salhany, J. M. (1979). Subunit inequivalence in super-oxide anion formation during photooxidation of human oxyhemoglobin. J. Biol. Chem. 254, 4532-4535.
8. Emsley, P. E. (1991). D.Phil thesis. University of York.
9. Gelin, B. R. & Karplus, M. (1977). Mechanism of tertiary structure change in hemoglobin. Proc. Natl Acad. Sci. USA, 74, 801-805.
10. Hiebl, I., Weber, R. E., Schneegans, D. & Braunitzer, G. (1989), High-altitude respiration of falconiformes. The primary structures and functional properties of the major and minor hemoglobin components of the adult white-headed vulture (Trigonoceps occipitalis, Aegipiinae). Biol. Chem Hoppe-Seyler, 370, 699-706.
11. Imai, K., Shih, D. T.-B., Tame, J., Nagai, K. & Miyazaki, G. (1989). Structural and functional consequences of amino acid substitutions in hemoglobin as manifested in natural and artificial mutants. Protein Seq. Data Anal. 2, 81-86.
12. Jessen, T.-H., Weber, R. E., Fermi, G., Tame, J. & Braunitzer, G. (1991). Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering. Proc. Natl Acad. Sci. USA, 88, 6519-6522.
13. Jones, T. A. (1982). In Computational Crystallography, pp. 3303-3317, Clarendon Press, Oxford.
14. Jones, T. A. & Kjeldgaard, M. (1991). O - The Manual. Uppsala University, Sweden.
15. Kimura, M. (1979). The neutral theory of molecular evolution. Sci. Amer. 241, 94-104.
16. Kleinschmidt, T. & Sgouros, J. G. (1987). Hemoglobin sequences. Biol. Chem. Hoppe-Seyler 368, 579-615.
17. Komiyama, N. H., Miyazaki, G., Tame, J. & Nagai, K. (1995). Transplanting a unique allosteric effect from crocodile into human haemoglobin. Nature, 373, 244-246.
18. Konnert, J. K. & Hendrickson, W. A. (1980). A restrained parameter thermal-factor refinement procedure. Acta Crystallog. sect. A, 36, 344-349.
19. Lamzin, V. S. & Wilson, K. S. (1993). Automated refinement of protein models. Acta Crystallog. sect. D, 49, 129-147.
20. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
21. Luisi, B. F. & Nagai, K. (1986). Crystallographic analysis of mutant haemoglobins made in Escherichia coli. Nature, 320, 555-556.
22. Mansouri, A. & Winterhalter, K. H. (1973). Nonequivalence of chains in hemoglobin oxidation. Biochemistry, 12, 4946-4949.
23. Matsuura, Y. (1991). AUTOMR: an automatic processing program system for the molecular replacement method. J. Appl. Crystallog. 24, 1063-1066.
24. Obertheur, W., Braunitzer, G. & Wuerdunger, I. (1982). Das Haemoglobin des Streifengans (Anser indicus). Primaerstruktur und Physiologie det Atmung, Stematik und Evolution. Hoppe-Seyler's Z. Physiol. Chem. 363, 581-590.
25. Olson, J. S., Mathews, A. J., Rohlfs, R. J., Springer, B. A., Edeberg, K. D., Tame, J., Renaud, J. P. & Nagai, K. (1988). The role of the distal histidine in myoglobin and haemoglobin. Nature, 336, 265-266.
26. Perutz, M. F. (1970a) Stereochemistry of cooperative effects in haemoglobin. Nature, 228, 726-734.
27. Perutz, M. F. (1970b). The Bohr effect and combination with organic phosphates. Nature, 228, 734-739.
28. Perutz, M. F. (1983). Species adaptation in a protein molecule. Mol. Biol. Evol. 1, 1-28.
29. Perutz, M. F., Fermi, G., Luisi, B. F., Shaanan, B. & Liddington, R. C. (1987). Stereochemistry of cooperative effects in haemoglobin. Acc. Chem. Res. 20, 309-321.
30. Petschow, D., Wuerdinger, I., Baumann, R., Duhm, J., Braunitzer, G. & Bauer, C. (1977). Causes of high blood oxygen affinity of animals living at high altitude. J. Appl. Physiol. 42, 139-143.
31. Richard, V., Dodson, G. G. & Mauguen, Y. (1993). Human deoxyhemoglobin-2,3 diphosphoglycerate complex low salt structure at 2.5 Å resolution. J. Mol. Biol. 233, 270-274.
32. Rollema, H. S. & Bauer, C. (1979). The interaction of inositol pentaphosphate with the hemoglobins of highland and lowland geese. J. Biol. Chem. 254, 12038-12043.
33. Sakabe, N. (1983). A focusing Weissenberg camera with multi-layer-line screens for macromolecular crystallography. J. Appl. Crystallog. 16, 542-547.
34. Shaanan, B. (1983). Structure of human oxyhemoglobin at 2.1 Å resolution. J. Mol. Biol. 171, 31-59.
35. Shih, D. T., Luisi, B. F., Miyazaki, G., Perutz, M. F. & Nagai, K. (1993). A mutagenic study of the allosteric linkage of His(HC3)146β in haemoglobin. J. Mol. Biol. 230, 1291-1296.
36. Swan, L. W. (1970). Goose of the Himalayas, Nat. Hist. 79, 68-75.
37. Tamburrini, M., Condo, S. G., di Prisco, G. & Giardina, B. (1994). Adaptation to extreme environments: structure-function relationship in emperor penguin haemoglobin. J. Mol. Biol. 237, 615-621.
38. Weber, R. E., Hiebl, I. & Braunitzer, G. (1988). High altitude and hemoglobin function in the vultures Gyps rueppelli and Aegypius monachus. Biol. Chem. Hoppe-Seyler, 369, 233-240.
39. 55-Ser): functions related to high-altitude respiration in geese. J. Appl. Physiol. 75, 2646-2655.