Crystalline ligand transitions in lamprey hemoglobin: Structural evidence for the regulation of oxygen affinity

Journal of Biological Chemistry

Volumn 276, Issue 28, 2001, Pages 26230-26236

  Heaslet, Holly A ^a,b   Royer Jr , William E ^a,c  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b CLARK UNIVERSITY   (United States)

^c BASF Bioresearch Corporation   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CARBON MONOXIDE; CRYSTAL STRUCTURE; DIMERIZATION; HEMOGLOBIN; HYDROGEN BONDS; OLIGOMERS; PROTONS;

DIMERIC INTERFACE;

BIOCHEMISTRY;

CARBON MONOXIDE; HEMOGLOBIN; LIGAND; OXYGEN;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; DIMERIZATION; HYDROGEN BOND; LAMPREY; LIGAND BINDING; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; STEREOCHEMISTRY; X RAY DIFFRACTION; ANIMAL; CHEMISTRY; CRYSTALLIZATION; METABOLISM; PROTEIN CONFORMATION;

MAMMALIA; PETROMYZON MARINUS; PETROMYZONTIDAE;

ANIMALS; CRYSTALLIZATION; HEMOGLOBINS; LAMPREYS; LIGANDS; OXYGEN; PROTEIN CONFORMATION;

EID: 0035854658     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M101391200     Document Type: Article

References (31)

1. Perutz, M. F., Fermi, G., Luisi, B., Shaanan, B., and Liddington, R. C. (1987) Acc. Chem. Res. 20, 309-321
2. Royer, W. E., Jr. (1994) J. Mol. Biol. 235, 657-681
3. Riggs, A. (1972) in The Biology of Lampreys (Hardisty, M. W., and Potter, I. C., eds) Vol. 2, pp. 261-286, Academic Press, Inc., London, UK
4. Heaslet, H. A., and Royer, W. E. (1999) Structure 7, 517-526
5. Wald, G., and Riggs, A. (1951) J. Gen. Physiol. 35, 45-53
6. Honzatko, R. B., Hendrickson, W. A., and Love, W. E. (1985) J. Mol. Biol. 184, 147-164
7. Barrick, D., Ho, N. T., Simplaceanu, V., Dahlquist, F. W., and Ho, C. (1997) Nat. Struct. Biol. 4, 78-83
8. Pardanani, A., Gibson, Q. H., Colotti, G., and Royer, W. E., Jr. (1997) J. Biol. Chem. 272, 13171-13179
9. Hendrickson, W. A., Love, W. E., and Murray, G. C. (1968) J. Mol. Biol. 33, 829-842
10. Otwinowski, Z., and Wladek, M. (1997) Methods Enzymol. 276, 307-326
11. Collaborative Computing Project, Number 4. (1994) Acta Crystallogr. Sec. D 50, 760-763
12. Navaza, J. (1994) Acta Crystallogr. Sec. A 50, 157-163
13. Brünger, A. T., Adams, P., Clore, M., Gros, P., Nilges, M., and Read, R. (1998) Acta Crystallogr. Sec. D 54, 905-921
14. Brünger, A. T. (1992) Nature 355, 471-475
15. Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sec. A 47, 110-119
16. Kleywegt, G. J., and Jones, T. A. (1994) in From First Map to Final Model (Bailey, S., Hubbard, R., and Waller, D. A., eds) pp. 59-66, Science and Engineering Council Daresbury Laboratory, Warrington, UK
17. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
18. Briehl, R. W. (1963) J. Biol. Chem. 238, 2361-2366
19. Andersen, M. E., and Gibson, Q. H. (1971) J. Biol. Chem. 246, 4790-4799
20. Dohi, Y., Sugita, Y., and Yoneyama, Y. (1973) J. Biol. Chem. 248, 2354-2363
21. Qiu, Y., Maillett, D. H., Knapp, J., Olson, J. S., and Riggs, A. F. (2000) J. Biol. Chem. 275, 13517-13528
22. Yang, F., and Phillips, G. N., Jr. (1996) J. Mol. Biol. 256, 762-774
23. Romo, T. D., Clarage, J. B., Sorensen, D. C., and Phillips, G. N., Jr. (1995) Proteins 22, 311-321
24. Vojtechovsky, J., Chu, K., Berendzen, J., Sweet, R. M., and Schlichting, I. (1999) Biophys. J. 77, 2153-2174
25. Kachalova, G. S., Popov, A. N., and Bartunik, H. D. (1999) Science 284, 473-479
26. Scott, E. E., Gibson, Q. H., and Olson, J. S. (2001) J. Biol. Chem. 276, 5177-5188
27. Li, T., Quillin, M. L., Phillips, G. N., and Olson, J. S. (1994) Biochemistry 33, 1433-1446
28. Esnouf, R. M. (1997) J. Mol. Graphics 15, 132-134
29. Merritt, E. A., and Bacon, D. J. (1997) Methods Enzymol. 277, 505-524
30. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
31. Ferrin, T. E., Huang, C. C., Jarvis, L. E., and Langridge, R. (1988) J. Mol. Graphics 6, 13-27