High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin

Journal of Molecular Biology

Volumn 234, Issue 1, 1993, Pages 140-155

  Quillin, Michael L ^a   Arduini, Robert M ^a   Olson, John S ^a   Phillips, George N ^a  

^a RICE UNIVERSITY   (United States)

Author keywords

Heme proteins; Ligand binding; Site directed mutagenesis; Sperm whale myoglobin; X ray crystallography

Indexed keywords

HISTIDINE; MUTANT PROTEIN; MYOGLOBIN;

ARTICLE; CRYSTAL STRUCTURE; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; WHALE; X RAY CRYSTALLOGRAPHY;

ANIMAL; CRYSTALLOGRAPHY, X-RAY; IRON; KINETICS; LIGANDS; METMYOGLOBIN; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.; SUPPORT, U.S. GOV'T, P.H.S.; WATER; WHALES;

EID: 0027368854     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1993.1569     Document Type: Article

References (30)

1. Bolognesi, M., Onesti, S., Gatti, G., Coda, A., Ascenzi, P. & Brunori, M. (1989). Aplysia limacma myoglobin: crystallographic analysis at L6 A resolution. J. Mol. Biol. 205, 529-544.
2. Brantley, R. E., Smerdon, S. J., WIIkinson, A. J., Singleton, E. W. & Olson, J. S. (1993). The mechanism of autooxidation of myoglobin. J. Biol. Chem. 268, 6995-7010.
3. Braunstein, D., Ansari, A., Berezden, J., Cowen, B. R., Egeberg, K. D., Frauenfelder, H., Hong, M. K., Ormos, R., Sauke, T. B., Scholl, R., Schulte, A., Sligar, S. G., Springer, B. A., Steinbach, P. J. & Young, R. D. (1988). Ligand binding to synthetic mutant myoglobin (His-E7→Gly): role of the distal histidine. Proc. Nat. Acad. Sci., U.S.A. 85, 8497-8501.
4. Briinger, A. (1987). Crystallographic R factor refinement by molecular dynamics. Science, 235, 458-460.
5. Carver, T. E., Rohlfs, R. S., Olson, J. S., Gibson, Q. H., Blackmore, R. S., Springer, B. A. & Sligar, S. G. (1990). Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques. J. Biol. Chem. 265, 20007-20020.
6. Collman, J. P. (1977). Synthetic models for the oxygenbinding hemoproteins. Acds Chem. Res. 10, 265-273.
7. Finzel, B. C. (1987). Incorporation of fast Fourier transforms to speed restrained least-squares refinement of protein structures. J. Appl. Crystallogr. 20, 53-55.
8. Giacometti, G. M., Ascenzi, P, Bolognesi, SI. & Brunori, M. (1981), Reactivity of ferric Aplysia myoglobin towards anionic ligands in the acidic region: proposal for a structural model. J. Mol. Biol. 146, 363-374.
9. Ikeda-Saito, M., Hori, H., Andersson, L. A., Prince, R. C., Pickering, I. J., George, G. N., Saunders, C. R. II, Lutz, R. S., Mc Kelvey, E. J., & Maltera, R. (1992).Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants. J. Biol. Chem. 267, 22843-22852.
10. Kabsch, W. (1988). Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector, J. Appl. Crystallogr. 21, 916-924.
11. Kuriyan, J., WIIz, S., Karplus, M. & Petsko, G. A. (1986). X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at L5 A resolution. J. Mol. Biol. 192, 133-154.
12. Morikis, D., Champion, P., Springer, B. A, & Sligar, S. G. (1989). Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry, 28, 4791-4800.
13. Morikis, IX, Champion, P., Springer, B. A., Egeberg, K. D. & Sligar, S. G. (1990). Resonance Raman studies of iron spin and axial coordination in distal pocket mutants of ferric myoglobin. J. Biol. Chem. 265, 12143-12145.
14. Oldfield, E., Guo, K., Augspurger, J. D. & Dykstra, C. E. (1991). A molecular model for the major conformational substates in heme proteins. J. Amer. Chem. Soc. 113, 7537-7541.
15. Ormos, P., Ansari, A., Braunstein, D., Cowen, B. R., Frauenfelder, H., Hong, M. K., Iben, I. E. T., Sauke, T. B., Steinbach, P. J. & Young, R. D. (1987), Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin: the connection between spectral and functional heterogeneity. Biophys. Chem. 57, 191-199.
16. Perutz, M. F. (1970). Stereochemistry of cooperative effects in haemoglobin. Nature (London), 228, 726-739.
17. Philips, G. N. Jr (1990). Comparison of the dynamics of myoglobin in different crystal forms. Biophys. J. 57, 381-383.
18. Philips, G. N. Jr, Arduini, R. A., Springer, B. A. & Sligar, S. G. (1990). Crystal structure of myoglobin from a synthetic gene. Proteins: Struct. Fund. Genet. 7, 358-365.
19. Philips, S. E. V, (1980). Structure and refinement of oxymyoglobin at 16 A resolution. J. Mol. Biol. 142, 531-554.
20. Philips, S. E. V. (1981). The X-ray structure of deoxy-Mb (pH 8-5) at 1-4 A resolution, Brookhaven Protein Data Bank, Brookhaven National Laboratories, New York.
21. Rajarathnam, K., La Mar, G. N., Chiu, M. L., Sligar, S. G., Singh, J. P. & Smith, K. M. (1991). Determination of the orientation of the magnetic axes of the cyano-metMb complexes of point mutants of myoglobin by solution NMR: influence of HisE7→ Gly and ArgCD3→ Giy substitutions. J. Amer. Chem. Soc. 113, 7886-7892.
22. Remington, S., Wiegand, G. & Huber, R. (1982). Crystallographic refinement and atomic models of two different forms of citrate synthase at 2-7 and 1-7 A resolution. J. Mol. Biol. 158, 111-152.
23. Rohlfs, R. J., Mathews, A. J., Carver, T. E., Olson, J. S., Springer, B. A., Egeberg, K. D. & Sligar, S. G. (1990). The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin. J. Biol. Chem. 265, 3168-3176.
24. Sack, J. S. (1988). CHAIN-A crystallographic modeling program. J. Mol. Graph. 6, 244-245.
25. Shimada, H. & Caughey, W. S. (1982). Dynamic protein structures: effects of pH on conformer stabIIities at the ligand-binding site of bovine heart myoglobin carbonyl. J. Biol. Chem. 257, 11893-11900.
26. 68 (Ell) mutant. Biochemistry, 30, 6252-6260.
27. Springer, B. A. & Sligar, S. G. (1987). High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Nat. Acad. Set., U.S.A. 84, 8961-8965.
28. Springer, B. A., Egeberg, K. D., Sligar, S. G., Rohlfs, R. J., Mathews, A. J. & Olson, J. S. (1989). Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. J. Biol. Chevi. 264, 3057-3060.
29. Takano, T. (1977a). Structure of myoglobin refined at 2'0 A resolution: T. Crystallographic refinement of metmvoglobin from sperm whale. J. Mol. Biol. 110. 537-568.
30. Takano, T. (1976) Structure of myoglobin refined at 20 A resolution. II. Structure of deoxymvoglobin from sperm whale. J. Mol. Biol. 110, 569-584.