Journal of Microbiology and Biotechnology

  • 제18권1호
  • /
  • Pages.59-62
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  • 2008
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

Overexpression, Purification, and Preliminary X-Ray Crystallographic Studies of Methionine Sulfoxide Reductase B from Bacillus subtilis

  • Park, Ae-Kyung (Division of Biotechnology, College of Life Sciences, Korea University) ;
  • Shin, Youn-Jae (Division of Biotechnology, College of Life Sciences, Korea University) ;
  • Moon, Jin-Ho (Division of Biotechnology, College of Life Sciences, Korea University) ;
  • Kim, Young-Kwan (Division of Biotechnology, College of Life Sciences, Korea University) ;
  • Hwang, Kwang-Yeon (Division of Biotechnology, College of Life Sciences, Korea University) ;
  • Chi, Young-Min (Division of Biotechnology, College of Life Sciences, Korea University)
  • 발행 : 2008.01.31
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초록

The peptide methionine sulfoxide reductases (Msrs) are enzymes that catalyze the reduction of methionine sulfoxide back to methionine. Because of two enantiomers of methionine sulfoxide (S and R forms), this reduction reaction is carried out by two structurally unrelated classes of enzymes, MsrA (E.C. 1.8.4.11) and MsrB (E.C. 1.8.4.12). Whereas MsrA has been well characterized structurally and functionally, little information on MsrB is available. The recombinant MsrB from Bacillus subtilis has been purified and crystallized by the hanging-drop vapor-diffusion method, and the functional and structural features of MsrB have been elucidated. The crystals belong to the trigonal space group P3, with unit-cell parameters a=b=136.096, $c=61.918{\AA}$, and diffracted to $2.5{\AA}$ resolution using a synchrotron-radiation source at Pohang Light Source. The asymmetric unit contains six subunits of MsrB with a crystal volume per protein mass $(V_M)\;of\;3.37{\AA}^3\;Da^{-1}$ and a solvent content of 63.5%.

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참고문헌

  1. Boschi-Muller, S., S. Azza, S. Sanglier-Cianferani, F. Talfournier, A. Van Dorsselear, and G. Branlant. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J. Biol. Chem. 275: 35908-35913 https://doi.org/10.1074/jbc.M006137200
  2. Brot, N., L. Weissbach, J. Werth, and H. Weissbach. 1981. Enzymatic reduction of protein-bound methionine sulfoxide. Proc. Natl. Acad. Sci. USA 78: 2155-2158
  3. Grimaud, R., B. Ezraty, J. K. Mitchell, D. Lafitte, C. Briand, P. J. Derrick, and F. Barras. 2001. Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase. J. Biol. Chem. 276: 48915-48920 https://doi.org/10.1074/jbc.M105509200
  4. Kryukov, G. V., R. A. Kumar, A. Koc, Z. Sun, and V. N. Gladyshev. 2002. Selenoprotein R is a zinc-containing stereospecific methionine sulfoxide reductase. Proc. Natl. Acad. Sci. USA 99: 4245-4250
  5. Kumar, R. A., A. Koc, R. L. Cerny, and V. N. Gladyshev. 2002. Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase. J. Biol. Chem. 277: 37527-37535 https://doi.org/10.1074/jbc.M203496200
  6. Lescure, A., D. Gautheret, P. Carbon, and A. Krol. 1999. Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J. Biol. Chem. 274: 38147-38154 https://doi.org/10.1074/jbc.274.53.38147
  7. Lowther, W. T., H. Weissbach, F. Etienne, N. Brot, and B. W. Matthews. 2002. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat. Struct. Biol. 9: 348-352
  8. Lowther, W. T., N. Brot, H. Weissbach, J. F. Honek, and B. W. Matthews. 2000. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proc. Natl. Acad. Sci. USA 97: 6463-6468
  9. Moskovitz, J., B. S. Berlett, J. M. Poston, and E. R. Stadtman. 1997. The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc. Natl. Acad. Sci. USA 94: 9585-9589
  10. Moskovitz, J., J. M. Poston, B. S. Berlett, N. J. Nosworthy, R. Szczepanowski, and E. R. Stadtman. 2000. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 275: 14167-14172 https://doi.org/10.1074/jbc.275.19.14167
  11. Olry, A., S. Boschi-Muller, M. Marraud, S. Sanglier-Cianferani, A. Van Dorsselear, and G. Branlant. 2002. Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis. J. Biol. Chem. 277: 12016-12022 https://doi.org/10.1074/jbc.M112350200
  12. Otwinowski, Z. and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326 https://doi.org/10.1016/S0076-6879(97)76066-X
  13. Sharov V. S., D. A. Ferrington, T. C. Squier, and C. Schoneich. 1999. Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase. FEBS Lett. 455: 247-250 https://doi.org/10.1016/S0014-5793(99)00888-1
  14. Tatusova, T. A. and T. L. Madden. 1999. Blast 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174: 247-250 https://doi.org/10.1111/j.1574-6968.1999.tb13575.x