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Volumn 335, Issue 4, 2004, Pages 1131-1141

Crystal Structure of MshB from Mycobacterium tuberculosis, a Deacetylase Involved in Mycothiol Biosynthesis

Author keywords

Crystal structure; Deacetylase; Enzyme mechanism; Mycothiol biosynthesis; Tuberculosis

Indexed keywords

ALANYLHISTIDYLPROLYLASPARTYLASPARTYLGLUTAMIC ACID; BACTERIAL ENZYME; BETA OCTYL GLUCOSIDE; DEACETYLASE; GLUTAMIC ACID DERIVATIVE; GLYCOSYLPHOSPHATIDYLINOSITOL; MYCOTHIOL; N ACETYLGLUCOSAMINE; OCTYL GLUCOSIDE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0346493029     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.034     Document Type: Article
Times cited : (59)

References (38)
  • 1
    • 0028469774 scopus 로고
    • Structure of a novel disulfide of 2-(N-acetylcysteinyl)amido-2-deoxy- alpha-D-glucopyranosyl-myo-inositol produced by Streptomyces sp
    • Sakuda S., Zhou Z.Y., Yamada Y. Structure of a novel disulfide of 2-(N-acetylcysteinyl)amido-2-deoxy-alpha-D-glucopyranosyl-myo-inositol produced by Streptomyces sp. Biosci. Biotechnol. Biochem. 58:1994;1347-1348.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1347-1348
    • Sakuda, S.1    Zhou, Z.Y.2    Yamada, Y.3
  • 2
    • 9244225687 scopus 로고    scopus 로고
    • Distribution of thiols in microorganisms: Mycothiol is a major thiol in most actinomycetes
    • Newton G., Arnold K., Price M., Sherrill C., Delcardayre S., Aharonowitz Y., et al. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J. Bacteriol. 178:1996;1990-1995.
    • (1996) J. Bacteriol. , vol.178 , pp. 1990-1995
    • Newton, G.1    Arnold, K.2    Price, M.3    Sherrill, C.4    Delcardayre, S.5    Aharonowitz, Y.6
  • 3
    • 0030942708 scopus 로고    scopus 로고
    • Mycothiol, 1-O-(2′-[N-acetyl-L-cysteinyl]amido-2′-deoxy- alpha-D-glucopyranosyl)-D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase
    • Misset-Smits M., van Ophem P.W., Sakuda S., Duine J.A. Mycothiol, 1-O-(2′-[N-acetyl-L-cysteinyl]amido-2′-deoxy-alpha-D-glucopyranosyl) -D-myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase. FEBS Letters. 409:1997;221-222.
    • (1997) FEBS Letters , vol.409 , pp. 221-222
    • Misset-Smits, M.1    Van Ophem, P.W.2    Sakuda, S.3    Duine, J.A.4
  • 4
    • 0033533411 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase
    • Patel M.P., Blanchard J.S. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry. 38:1999;11827-11833.
    • (1999) Biochemistry , vol.38 , pp. 11827-11833
    • Patel, M.P.1    Blanchard, J.S.2
  • 5
    • 0034609546 scopus 로고    scopus 로고
    • A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase
    • Newton G.L., Av-Gay Y., Fahey R.C. A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry. 39:2000;10739-10746.
    • (2000) Biochemistry , vol.39 , pp. 10739-10746
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 6
    • 0032515068 scopus 로고    scopus 로고
    • Mycothiol biosynthesis and metabolism. Cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in Mycobacterium smegmatis
    • Anderberg S.J., Newton G.L., Fahey R.C. Mycothiol biosynthesis and metabolism. Cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in Mycobacterium smegmatis. J. Biol. Chem. 273:1998;30391-30397.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30391-30397
    • Anderberg, S.J.1    Newton, G.L.2    Fahey, R.C.3
  • 8
    • 0038662691 scopus 로고    scopus 로고
    • The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA)
    • Newton G.L., Koledin T., Gorovitz B., Rawat M., Fahey R.C., Av-Gay Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185:2003;3476-3479.
    • (2003) J. Bacteriol. , vol.185 , pp. 3476-3479
    • Newton, G.L.1    Koledin, T.2    Gorovitz, B.3    Rawat, M.4    Fahey, R.C.5    Av-Gay, Y.6
  • 9
    • 0034460953 scopus 로고    scopus 로고
    • N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis
    • Newton G.L., Av-Gay Y., Fahey R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2- deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182:2000;6958-6963.
    • (2000) J. Bacteriol. , vol.182 , pp. 6958-6963
    • Newton, G.L.1    Av-Gay, Y.2    Fahey, R.C.3
  • 10
    • 0037018946 scopus 로고    scopus 로고
    • ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D- glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases
    • Sareen D., Steffek M., Newton G.L., Fahey R.C. ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases. Biochemistry. 41:2002;6885-6890.
    • (2002) Biochemistry , vol.41 , pp. 6885-6890
    • Sareen, D.1    Steffek, M.2    Newton, G.L.3    Fahey, R.C.4
  • 11
    • 0036401562 scopus 로고    scopus 로고
    • Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes
    • Koledin T., Newton G.L., Fahey R.C. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch. Microbiol. 178:2002;331-337.
    • (2002) Arch. Microbiol. , vol.178 , pp. 331-337
    • Koledin, T.1    Newton, G.L.2    Fahey, R.C.3
  • 12
    • 0037245381 scopus 로고    scopus 로고
    • Inhibition and kinetics of Mycobacterium tuberculosis and Mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors
    • Nicholas G.M., Eckman L.L., Newton G.L., Fahey R.C., Ray S., Bewley C.A. Inhibition and kinetics of Mycobacterium tuberculosis and Mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors. Bioorg. Med. Chem. 11:2003;601-608.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 601-608
    • Nicholas, G.M.1    Eckman, L.L.2    Newton, G.L.3    Fahey, R.C.4    Ray, S.5    Bewley, C.A.6
  • 13
    • 0033119014 scopus 로고    scopus 로고
    • Mammalian PIG-L and its yeast homologue Gpi12p are N- acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis
    • Watanabe R., Ohishi K., Maeda Y., Nakamura N., Kinoshita T. Mammalian PIG-L and its yeast homologue Gpi12p are N- acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339:1999;185-192.
    • (1999) Biochem. J. , vol.339 , pp. 185-192
    • Watanabe, R.1    Ohishi, K.2    Maeda, Y.3    Nakamura, N.4    Kinoshita, T.5
  • 14
    • 10744228324 scopus 로고    scopus 로고
    • Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8
    • Handa N., Terada T., Kamewari Y., Hamana H., Tame J.R.H., Park S.-Y., et al. Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8. Protein Sci. 12:2003;1621-1632.
    • (2003) Protein Sci. , vol.12 , pp. 1621-1632
    • Handa, N.1    Terada, T.2    Kamewari, Y.3    Hamana, H.4    Tame, J.R.H.5    Park, S.-Y.6
  • 15
    • 0345306583 scopus 로고    scopus 로고
    • The crystal structure of 1D-myo-inosityl 2-acetamido-2-deoxy-α-D- glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold
    • Maynes J.T., Garen C., Cherney M.M., Newton G., Arad D., Av-Gay Y., et al. The crystal structure of 1D-myo-inosityl 2-acetamido-2-deoxy-α-D- glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278:2003;47166-47170.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47166-47170
    • Maynes, J.T.1    Garen, C.2    Cherney, M.M.3    Newton, G.4    Arad, D.5    Av-Gay, Y.6
  • 16
  • 17
    • 0346651485 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of N-acetyl-1-D-myo- inosityl-2-deoxy-α-D-glucopyranoside deacetylase from Mycobacterium tuberculosis
    • McCarthy A.A., Knijff R., Peterson N.A., Baker E.N. Crystallization and preliminary X-ray analysis of N-acetyl-1-D-myo-inosityl-2-deoxy-α-D- glucopyranoside deacetylase from Mycobacterium tuberculosis. Acta Crystallog. sect. D. 59:2003;2316-2318.
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 2316-2318
    • McCarthy, A.A.1    Knijff, R.2    Peterson, N.A.3    Baker, E.N.4
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0034642186 scopus 로고    scopus 로고
    • The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
    • Campbell R.E., Mosimann S.C., Tanner M.E., Strynadka N.C.J. The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases. Biochemistry. 39:2000;14993-15001.
    • (2000) Biochemistry , vol.39 , pp. 14993-15001
    • Campbell, R.E.1    Mosimann, S.C.2    Tanner, M.E.3    Strynadka, N.C.J.4
  • 20
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha S., Walker D., Shi Y., Walker S. The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. 9:2000;1045-1052.
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 21
    • 0035976715 scopus 로고    scopus 로고
    • Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
    • Wrabl J.O., Grishin N.V. Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. J. Mol. Biol. 314:2001;365-374.
    • (2001) J. Mol. Biol. , vol.314 , pp. 365-374
    • Wrabl, J.O.1    Grishin, N.V.2
  • 22
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin M.S., Donigian J.R., Cohen A., Richon V.M., Rifkind R.A., Marks P.A., et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature. 401:1999;188-193.
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 25
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews B.W. Structural basis of the action of thermolysin and related zinc peptidases. Accts. Chem. Res. 21:1988;333-340.
    • (1988) Accts. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 26
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 26:1993;795-800.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 28
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Uson I., Sheldrick G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9:1999;643-648.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 29
    • 0031058188 scopus 로고    scopus 로고
    • Heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., Bricogne G. Heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 30
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallog. sect. D. 56:2000;965-972.
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 31
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-255.
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6:1999;458-463.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 35
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A.T. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 37
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


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