Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin βα, at 2.5 Å resolution

Journal of Molecular Biology

Volumn 287, Issue 2, 1999, Pages 369-382

  Shirai, Tsuyoshi ^a   Fujikake, Masahiro ^a   Yamane, Takashi ^a   Inaba, Kenji ^b   Ishimori, Koichiro ^b   Morishima, Isao ^b  

^a NAGOYA UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

Author keywords

Chimeric protein; Protein engineering; Protein evolution; Structural unit; X ray crystallography

Indexed keywords

CHIMERIC PROTEIN; HEMOGLOBIN; HEMOGLOBIN ALPHA CHAIN; HEMOGLOBIN BETA CHAIN;

ARTICLE; CRYSTAL STRUCTURE; EXON; PRIORITY JOURNAL; PROTEIN CONFORMATION; STEREOSPECIFICITY;

EID: 0033605874     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2603     Document Type: Article

References (40)

1. Blake C. C. F. Exons encode protein functional units. Nature. 277:1979;598.
2. Borgstahl G. E. O., Rogers P. H., Arnone A. The 1.8 Å structure of carbonmonoxy-β4 hemoglobin: analysis of a homotetramer with the R quaternary structure of liganded α2β2 hemoglobin. J. Mol. Biol. 236:1994a;817-830.
3. Borgstahl G. E. O., Rogers P. H., Arnone A. The 1.9 Å structure of deoxyβ4 hemoglobin: analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure. J. Mol. Biol. 236:1994b;831-843.
4. Brünger A. T. X-PLOR Version 3.1. A system for X-ray Crystallography and NMR. 1992;Yale University Press, New Haven and London.
5. Cambillau C. Turbo-FRODO, Molecular Graphics Program for Silicon Graphics IRIS 4D Series, Version 3.0. 1992;Bio-Graphics, Marseille.
6. 2binding properties of the product of the central exon of β-globin gene. Nature. 291:1981;87-90.
7. Cusack S. Eleven down and nine to go. Nature Struct. Biol. 2:1995;824-831.
8. Dickerson R. E., Geis I. Hemoglobin: Structure, Evolution and Pathology. 1983;The Benjamin/Cummings Publishing Company, Inc.
9. Eliezer D., Yao J., Dyson H. J., Wright P. E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol. 5:1998;148-155.
10. Fermi G., Perutz M. F., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175:1984;159-174.
11. Fukami-Kobayashi K., Mizutani M., Go M. Correlation between module boundaries and intron positions in hemoglobins from various taxa. Go M., Schimmel P. Tracing Biological Evolution in Protein and Gene Structures. 1995;271-282 Elsevier, Amsterdam.
12. Gilbert W. Why genes in pieces? Nature. 271:1978;501.
13. Gilbert W. The exon theory of genes. Cold Spring Harbor Symp. Quant. Biol. 52:1987;901-905.
14. Go M. Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature. 291:1981;90-92.
15. Go M. Protein structures and split genes. Advan. Biophys. 19:1985;91-131.
16. Goodman M., Moore W., Matsuda G. Darwinian evolution in the genealogy of haemoglobin. Nature. 253:1975;603-608.
17. Hubbard S. R., Hendrickson W. A., Lambright D. G., Boxer S. G. X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 Å resolution. J. Mol. Biol. 213:1990;215-218.
18. Hughson F. M., Wright P. E., Baldwin R. L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548.
19. Hurst L. D. The uncertain origin of introns. Nature. 371:1994;381-382.
20. Inaba K., Wakasugi K., Ishimori K., Konno T., Kataoka M., Morishima I. Structural and functional roles of modules in hemoglobin. J. Biol. Chem. 272:1997;30054-30060.
21. Inaba K., Ishimori K., Imai K., Morishima I. Structural and functional effects of pseudo-module substitution in hemoglobin subunits: New structural and functional units in globin structure. J. Biol. Chem. 273:1998a;8384-8388.
22. Inaba K., Ishimori K., Morishima I. Structural and functional roles of heme binding module in globin proteins - identification of the segment regulating the heme binding structure. J. Mol. Biol. 283:1998b;311-327.
23. Jellie A. M., Tate W. P., Trotman C. N. A. Evolutionary history of introns in a multidomain globin gene. J. Mol. Evol. 42:1996;641-647.
24. Jennings P. A., Wright P. E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896.
25. Kohlstaedt L. A., Wang J., Friedman J. M., Rice P. A., Steitz T. A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science. 256:1992;1783-1790.
26. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
27. Kumagai I., Takeda S., Miura K. Functional conversion of the homologous proteins α-lactalbumin and lysozyme by exon exchange. Proc. Natl Acad. Sci. USA. 89:1992;5887-5891.
28. Logsdon J. M., Palmer J. D., Stoltzfus A. Origin of introns - early or late? Nature. 369:1994;526-527.
29. Long M., de Souza S. J., Gilbert W. Evolution of the intron-exon structure of eukaryotic genes. Curr. Biol. 5:1995;774-778.
30. Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:1970;726-739.
31. Rossmann M. G., Liljas A., Brändén C.-I., Banaszak L. J. Evolutionary and structural relationships among dehydrogenases. Boyer P. D. The Enzymes. 1975;62-102 Academic Press, New York.
32. Russell R. B. Domain insertion. Protein Eng. 7:1994;1407-1410.
33. Shaanan B. Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171:1983;31-59.
34. Shirai T., Fujikake M., Yamane T., Inaba K., Ishimori K., Morishima I. Design, construction, crystallization and preliminary X-ray analysis of a fine-tuning mutant (F133V) of a module-substituted chimera hemoglobin. Proteins: Struct. Funct. Genet. 32:1998;263-267.
35. Silva M. M., Rogers P. H., Arnone A. A third quaternary structure of human hemoglobin A at 1.7- Å resolution. J. Biol. Chem. 267:1992;17248-17256.
36. SH): determination of stoichiometries and equilibrium constants as a function of temperature. J. Biol. Chem. 252:1977;74-81.
37. Wakasugi K., Ishimori K., Imai K., Wada Y., Morishima I. "Module" substitution in hemoglobin subunits: preparation and characterization of a "chimera βα-subunit" J. Biol. Chem. 269:1994;18750-18756.
38. Wakasugi K., Ishimori K., Morishima I. "Module"-substituted globins: artificial exon shuffling among myoglobin, hemoglobin α- and β-subunits. Biophys. Chem. 68:1997;265-273.
39. Xia Z.-X., Mathews F. S. Molecular structure of flavocytochrome b 2 at 2.4 Å resolution. J. Mol. Biol. 212:1990;837-863.
40. Zhou M., Gomez-Sanchez C. E., Xue D., Foecking M. F. The hybrid rat cytochrome P450 containing the first 5 exons of the CYP11B1 and last 4 exons from the CYP11B2 enzyme retains 11β-hydroxylase activity, but the alternative hybrid is inactive. Biochem. Biophys. Res. Commun. 199:1994;130-135.