Solution structure of the Iγ subdomain of the Mu end DNA-binding domain of phage Mu transposase

Journal of Molecular Biology

Volumn 273, Issue 1, 1997, Pages 19-25

  Clubb, Robert T ^a,b   Schumacher, Silke ^a   Mizuuchi, Kiyoshi ^a   Gronenborn, Angela M ^a   Clore, G Marius ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Helix turn helix; I subdomain; Phage Mu; Solution structure; Transposase

Indexed keywords

DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; TRANSPOSASE;

ARTICLE; BACTERIOPHAGE MU; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

EID: 0031576325     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1312     Document Type: Article

References (32)

1. Bax A., Grzesiek S. Methodological advances in protein NMR. Acc. Chem. Res. 26:1993;131-138.
2. Bax A., Vuister G. W., Grzesiek S., Delaglio F., Wang A. C., Tschudin R., Zhu G. Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods Enzymol. 239:1994;79-105.
3. Brennan R. G. The winged-helix DNA-binding motif: another helix-turn-helix takeoff. Cell. 74:1993;773-776.
4. Brooks B. R., Bruccoleri R. E., Olafson B. D., States D. J., Swaminathan S., Karplus M. CHARMM: a program for macromolecuar energy minimizaion and dynamics calculations. J. Comput. Chem. 4:1993;187-217.
5. Brünger A. T. XPLOR 3.1: A System for X-ray Crystallography and NMR. 1993;Yale University Press, New Haven.
6. Clore G. M., Gronenborn A. M. Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science. 252:1991;1390-1399.
7. Clubb R. T., Omichinski J. G., Savilahti H., Mizuuchi K., Gronenborn A. M., Clore G. M. A novel class of winged helix-turn-helix protein: the DNA binding domain of Mu transposase. Structure. 2:1994;1041-1048.
8. Dekker N., Cox M., Boelens R., Verrijzer C. P., van der Vliet P. C., Kaptein R. Solution structure of the POU-specific DNA binding domain of Oct-1. Nature. 362:1993;852-855.
9. Delaglio F., Grzesiek S., Vuister G. W., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;277-293.
10. Garrett D. S., Powers R., Gronenborn A. M., Clore G. M. A common sense approach to peak picking in two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95:1991;214-220.
11. Garrett D. S., Kuszewski J., Hancock T. J., Lodi P. J., Vuister G. W., Gronenborn A. M., Clore G. M. The impact of direct refinement against three-bond NH-CαH coupling constants on protein structure determination by NMR. J. Magn. Reson. ser B. 104:1994;99-103.
12. 13. J. Biomol. NMR. 4:1994;455-458.
13. Kim K., Harshey R. M. Mutational analysis of the att DNA-binding domain of phage Mu transposase. Nucl. Acids Res. 23:1995;3937-3943.
14. Kissinger C. R., Liu B., Martin-Blanco E., Kornberg T. B., Pabo C. O. Crystal structure of an engrailed homeodomain-DNA complex at 2.8 Å resolution: a framework for understanding homeodomain-DNA interactions. 1990.
15. Klemm J. D., Rould M. A., Aurora R., Herr W., Pabo C. O. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell. 77:1994;21-32.
16. Konradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;52-55.
17. Kuo C. -F., Zou A., Jayaram M., Getzoff E., Harshey R. M. DNA-protein complexes during attachment-site synapsis in Mu DNA transposition. EMBO J. 10:1991;1585-1591.
18. 1313. J. Magn. Reson. ser. B. 106:1995;92-96.
19. Kuszewski J., Gronenborn A. M., Clore G. M. Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases. Protein Sci. 5:1996;1067-1080.
20. Kuszewski J., Gronenborn A. M., Clore G. M. Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids. J. Magn. Reson. 125:1997;171-177.
21. Laskowski R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
22. Lavoie B. D., Chaconas G. Transposition of phage Mu DNA. Curr. Top. Microbiol. Immunol. 204:1995;83-102.
23. Mizuuchi K. Transpositional recombination: mechanistic insights from studies of Mu and other elements. Annu. Rev. Biochem. 61:1992;1011-1051.
24. Mizuuchi M., Mizuuchi K. Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: implication for regulation. Cell. 58:1989;399-408.
25. Nilges M., Clore G. M., Gronenborn A. M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters. 229:1988;317-324.
26. 1. Biopolymers. 29:1990;813-822.
27. Pabo C. O., Sauer R. T. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1992;1053-1095.
28. Powers R., Garrett D. S., March C. J., Frieden E. A., Gronenborn A. M., Clore G. M. The high resolution three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy. Biochemistry. 32:1993;6744-6762.
29. Rice P. A., Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell. 82:1995;209-220.
30. Symonds N., Toussaint A., van de Putte P., Howe M. M. Phage Mu. 1987;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
31. Wright P. E. POU domains and homeodomains. Curr. Op. Struct. Biol. 4:1994;22-27.
32. Zou A., Leung P. C., Harshey R. M. Transposase contacts with Mu DNA ends. J. Biol. Chem. 266:1991;20476-20482.