Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair

Journal of Biochemistry

Volumn 126, Issue 6, 1999, Pages 986-990

  Nakagawa, Noriko ^a   Sugahara, Mitsuaki ^a,b   Masui, Ryoji ^a   Kato, Ryuichi ^a   Fukuyama, Keiichi ^a   Kuramitsu, Seiki ^a,b,c  

^a OSAKA UNIVERSITY   (Japan)

^b RIKEN SPring 8 Center   (Japan)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

Author keywords

Crystal structure; DNA repair enzyme; Nucleotide excision repair; Thermus thermophilus HB8; UvrB

Indexed keywords

DNA; HELICASE; NUCLEOTIDE; PROTEIN; RNA HELICASE;

ARTICLE; CRYSTAL STRUCTURE; EXCISION REPAIR; NONHUMAN; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; THERMUS THERMOPHILUS;

BACTERIA (MICROORGANISMS); THERMUS THERMOPHILUS;

EID: 0033376420     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022566     Document Type: Article

References (22)

1. Friedberg, E.C., Walker, G.C., and Siede, W. (1995) DNA Repair and Mutagenesis, American Society of Microbiology Press, Washington, DC
2. Grossman, L. and Thiagalingam, S. (1993) Nucleotide excision repair, a tracking mechanism in search of damage. J. Biol. Chem. 268, 16871-16874
3. Sancar, A. (1996) DNA excision repair. Annu. Rev. Biochem. 65, 43-81
4. Kato, R., Yamamoto, N., Kito, K., and Kuramitsu, S. (1996) ATPase activity of UvrB protein from Thermus thermophilus HB8 and its interaction with DNA. J. Biol. Chem. 271, 9612-9618
5. Nakagawa, N., Masui, R., Kato, R., and Kuramitsu, S. (1997) Domain structure of Thermos thermophilus UvrB protein. Similarity in domain structure to a helicase. J. Biol. Chem. 272, 22703-22713
6. Shibata, A., Nakagawa, N., Sugahara, M., Masui, R., Kato, R., Kuramitsu, S., and Fukuyama, K. (1998) Crystallization and preliminary X-ray diffraction studies of a DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8. Acta Crystallogr. D55, 704-705
7. Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
8. McRee, D.E. (1993) Practical Protein Crystallography, Academic Press, San Diego
9. Collaborative Computational Project, Number 4. (1994) The CCP4 suite: Program for protein crystallography. Acta Crystallogr. D50, 760-763
10. Jones, T.A., Zou, J.-Y., Cowan, S.W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. 21, 916-924
11. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T., and Warren, G.L. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905-921
12. Velankar, S.S., Soultanas, P., Dillingham, M.S., Subramanya, H.S., and Wigley, D.B. (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97, 75-84
13. Korolev, S., Hsieh, J., Gauss, G.H., Lohman, T.M., and Waksman, G. (1997) Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90, 635-647
14. Kim, J.L., Morgenstern, K.A., Griffith, J.P., Dwyer, M.D., Thomson, J.A., Murcko, M.A., Lin, C., and Caron, P.R. (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6, 89-100
15. Selby, C.P. and Sancar, A. (1995) Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J. Biol. Chem. 270, 4882-4889
16. Hsu, D.S., Kim, S.T., Sun, Q., and Sancar, A. (1995) Structure and function of the UvrB protein. J. Biol. Chem. 270, 8319-8327
17. Moolenaar, G.F., Franken, K.L.M.C., Dijkstra, D.M., Thomas-Oates, J.E., Visse, R., van de Putte, P., and Goosen, N. (1995) The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3′-incision. J. Biol. Chem. 270, 30508-30515
18. Gorbalenya, A.E. and Koonin, E.V. (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429
19. Gordienko, I. and Rupp, W.D. (1997) The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage. EMBO J. 16, 889-895
20. Zou, Y. and Van Houten, B. (1999) Strand opening by the Uvr-A2B complex allows dynamic recognition of DNA damage. EMBO J. 18, 4889-4901
21. Shi, Q., Thresher, R., Sancar, A., and Griffith, J. (1992) Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex. J. Mol. Biol. 226, 425-432
22. Orren, D.K. and Sancar, A. (1990) Formation and enzymatic properties of the UvrB-DNA complex. J. Biol. Chem. 266, 15796-15803