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Volumn 279, Issue 6, 2012, Pages 1093-1105

Structural characterization of Helicobacter pylori dethiobiotin synthetase reveals differences between family members

Author keywords

adenosine binding; biotin synthesis pathway; crystal structure; dethiobiotin synthesis; nucleotide recognition

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DETHIOBIOTIN SYNTHETASE; GUANOSINE TRIPHOSPHATASE; NUCLEOSIDE; UNCLASSIFIED DRUG;

EID: 84862804236     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08506.x     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 0037364908 scopus 로고    scopus 로고
    • Biotin in microbes, the genes involved in its biosynthesis, its biochemical role and perspectives for biotechnological production
    • Streit WR, &, Entcheva P, (2003) Biotin in microbes, the genes involved in its biosynthesis, its biochemical role and perspectives for biotechnological production. Appl Microbiol Biotechnol 61, 21-31. (Pubitemid 36458049)
    • (2003) Applied Microbiology and Biotechnology , vol.61 , Issue.1 , pp. 21-31
    • Streit, W.R.1    Entcheva, P.2
  • 2
    • 21444433993 scopus 로고    scopus 로고
    • Uptake, localization, and noncarboxylase roles of biotin
    • DOI 10.1146/annurev.nutr.25.121304.131724
    • Zempleni J, (2005) Uptake, localization, and noncarboxylase roles of biotin. Annu Rev Nutr 25, 175-196. (Pubitemid 41208999)
    • (2005) Annual Review of Nutrition , vol.25 , pp. 175-196
    • Zempleni, J.1
  • 3
    • 34248570123 scopus 로고    scopus 로고
    • Brave new (strept)avidins in biotechnology
    • DOI 10.1016/j.tibtech.2007.04.001, PII S0167779907000881
    • Laitinen OH, Nordlund HR, Hytonen VP, &, Kulomaa MS, (2007) Brave new (strept)avidins in biotechnology. Trends Biotechnol 25, 269-277. (Pubitemid 46755409)
    • (2007) Trends in Biotechnology , vol.25 , Issue.6 , pp. 269-277
    • Laitinen, O.H.1    Nordlund, H.R.2    Hytonen, V.P.3    Kulomaa, M.S.4
  • 4
    • 0346727529 scopus 로고    scopus 로고
    • Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
    • DOI 10.1126/science.1088493
    • Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, &, Drennan CL, (2004) Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303, 76-79. (Pubitemid 38055773)
    • (2004) Science , vol.303 , Issue.5654 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 5
    • 0035917898 scopus 로고    scopus 로고
    • Structural enzymology of biotin biosynthesis
    • DOI 10.1016/S0014-5793(01)02325-0, PII S0014579301023250
    • Schneider G, &, Lindqvist Y, (2001) Structural enzymology of biotin biosynthesis. FEBS Lett 495, 7-11. (Pubitemid 32367964)
    • (2001) FEBS Letters , vol.495 , Issue.1-2 , pp. 7-11
    • Schneider, G.1    Lindqvist, Y.2
  • 6
    • 0014963074 scopus 로고
    • The purification and properties of dethiobiotin synthetase
    • Krell K, &, Eisenberg MA, (1970) The purification and properties of dethiobiotin synthetase. J Biol Chem 245, 6558-6566.
    • (1970) J Biol Chem , vol.245 , pp. 6558-6566
    • Krell, K.1    Eisenberg, M.A.2
  • 7
    • 37049086848 scopus 로고
    • Mechanism of dethiobiotin synthetase - Characterization of the 8-aminocarbamate of (7r,8s)-7,8 diaminononanoate as an enzyme-bound intermediate
    • Baxter RL, Ramsey AJ, Mciver LA, &, Baxter HC, (1994) Mechanism of dethiobiotin synthetase-characterization of the 8-aminocarbamate of (7r,8s)-7,8 diaminononanoate as an enzyme-bound intermediate. J Chem Soc Chem Commun 5, 559-560.
    • (1994) J Chem Soc Chem Commun , vol.5 , pp. 559-560
    • Baxter, R.L.1    Ramsey, A.J.2    McIver, L.A.3    Baxter, H.C.4
  • 9
    • 0029645896 scopus 로고
    • Substrate binding and carboxylation by dethiobiotin synthetase - A kinetic and X-ray study
    • DOI 10.1016/S0969-2126(01)00256-8
    • Alexeev D, Baxter RL, Smekal O, &, Sawyer L, (1995) Substrate-binding and carboxylation by dethiobiotin synthetase-a kinetic and X-ray study. Structure 3, 1207-1215. (Pubitemid 3001426)
    • (1995) Structure , vol.3 , Issue.11 , pp. 1207-1215
    • Alexeev, D.1    Baxter, R.L.2    Smekal, O.3    Sawyer, L.4
  • 10
    • 0029118765 scopus 로고
    • Mechanism of an Atp-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate
    • Huang WJ, Jia J, Gibson KJ, Taylor WS, Rendina AR, Schneider G, &, Lindqvist Y, (1995) Mechanism of an Atp-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Biochemistry 34, 10985-10995.
    • (1995) Biochemistry , vol.34 , pp. 10985-10995
    • Huang, W.J.1    Jia, J.2    Gibson, K.J.3    Taylor, W.S.4    Rendina, A.R.5    Schneider, G.6    Lindqvist, Y.7
  • 11
    • 37049083953 scopus 로고
    • The mechanism of Escherichia coli dethiobiotin synthetase - The closure of the ureido ring of dethiobiotin involves formation of a carbamic-phosphate mixed anhydride
    • Baxter RL, &, Baxter HC, (1994) The mechanism of Escherichia coli dethiobiotin synthetase-the closure of the ureido ring of dethiobiotin involves formation of a carbamic-phosphate mixed anhydride. J Chem Soc Chem Commun 6, 759-760.
    • (1994) J Chem Soc Chem Commun , vol.6 , pp. 759-760
    • Baxter, R.L.1    Baxter, H.C.2
  • 12
    • 0030790705 scopus 로고    scopus 로고
    • Isolation and chemistry of the mixed anhydride intermediate in the reaction catalyzed by dethiobiotin synthetase
    • DOI 10.1021/bi970447t
    • Gibson KJ, (1997) Isolation and chemistry of the mixed anhydride intermediate in the reaction catalyzed by dethiobiotin synthetase. Biochemistry 36, 8474-8478. (Pubitemid 27305129)
    • (1997) Biochemistry , vol.36 , Issue.28 , pp. 8474-8478
    • Gibson, K.J.1
  • 13
    • 0028773464 scopus 로고
    • Crystal-structure of an Atp-dependent carboxylase, dethiobiotin synthetase, at 1.65-angstrom resolution
    • Huang WJ, Lindqvist Y, Schneider G, Gibson KJ, Flint D, &, Lorimer G, (1994) Crystal-structure of an Atp-dependent carboxylase, dethiobiotin synthetase, at 1.65-angstrom resolution. Structure 2, 407-414.
    • (1994) Structure , vol.2 , pp. 407-414
    • Huang, W.J.1    Lindqvist, Y.2    Schneider, G.3    Gibson, K.J.4    Flint, D.5    Lorimer, G.6
  • 14
    • 0034602364 scopus 로고    scopus 로고
    • Three-dimensional view of the surface motif associated with the P-loop structure: Cis and trans cases of convergent evolution
    • Via A, Ferre F, Brannetti B, Valencia A, &, Helmer-Citterich M, (2000) Three-dimensional view of the surface motif associated with the P-loop structure: Cis and trans cases of convergent evolution. J Mol Biol 303, 455-465.
    • (2000) J Mol Biol , vol.303 , pp. 455-465
    • Via, A.1    Ferre, F.2    Brannetti, B.3    Valencia, A.4    Helmer-Citterich, M.5
  • 15
    • 34347393442 scopus 로고    scopus 로고
    • Structural genomics: keeping up with expanding knowledge of the protein universe
    • DOI 10.1016/j.sbi.2007.06.003, PII S0959440X07000796, Nucleic acids / Sequences and topology
    • Grabowski M, Joachimiak A, Otwinowski Z, &, Minor W, (2007) Structural genomics: keeping up with expanding knowledge of the protein universe. Curr Opin Struct Biol 17, 347-353. (Pubitemid 47021368)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.3 , pp. 347-353
    • Grabowski, M.1    Joachimiak, A.2    Otwinowski, Z.3    Minor, W.4
  • 16
    • 0028774542 scopus 로고
    • Mechanistic implications and family relationships from the structure of dethiobiotin synthetase
    • Alexeev D, Baxter RL, &, Sawyer L, (1994) Mechanistic implications and family relationships from the structure of dethiobiotin synthetase. Structure 2, 1061-1072.
    • (1994) Structure , vol.2 , pp. 1061-1072
    • Alexeev, D.1    Baxter, R.L.2    Sawyer, L.3
  • 17
    • 77955234669 scopus 로고    scopus 로고
    • Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase
    • Dey S, Lane JM, Lee RE, Rubin EJ, &, Sacchettini JC, (2010) Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase. Biochemistry 49, 6746-6760.
    • (2010) Biochemistry , vol.49 , pp. 6746-6760
    • Dey, S.1    Lane, J.M.2    Lee, R.E.3    Rubin, E.J.4    Sacchettini, J.C.5
  • 18
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • Leipe DD, Wolf YI, Koonin EV, &, Aravind L, (2002) Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 317, 41-72. (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 20
    • 0030933184 scopus 로고    scopus 로고
    • Active site mutants of Escherichia coli dethiobiotin synthetase: Effects of mutations on enzyme catalytic and structural properties
    • DOI 10.1021/bi9631677
    • Yang G, Sandalova T, Lohman K, Lindqvist Y, &, Rendina AR, (1997) Active site mutants of Escherichia coli dethiobiotin synthetase: effects of mutations on enzyme catalytic and structural properties. Biochemistry 36, 4751-4760. (Pubitemid 27180955)
    • (1997) Biochemistry , vol.36 , Issue.16 , pp. 4751-4760
    • Yang, G.1    Sandalova, T.2    Lohman, K.3    Lindqvist, Y.4    Rendina, A.R.5
  • 21
    • 0031703554 scopus 로고    scopus 로고
    • 3-diaminopelargonic acid and enzyme-MgADP- dethiobiotin-phosphate; implications for catalysis
    • Kack H, Sandmark J, Gibson KJ, Schneider G, &, Lindqvist Y, (1998) Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin- phosphate; implications for catalysis. Protein Sci 7, 2560-2566. (Pubitemid 28565697)
    • (1998) Protein Science , vol.7 , Issue.12 , pp. 2560-2566
    • Kack, H.1    Sandmark, J.2    Gibson, K.J.3    Schneider, G.4    Lindqvist, Y.5
  • 22
    • 0034651543 scopus 로고    scopus 로고
    • When fold is not important: A common structural framework for adenine and AMP binding in 12 unrelated protein families
    • DOI 10.1002/(SICI)1097-0134(20000215)38:3<310::AID-PROT7>3.0.CO;2-T
    • Denessiouk KA, &, Johnson MS, (2000) When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families. Proteins 38, 310-326. (Pubitemid 30084340)
    • (2000) Proteins: Structure, Function and Genetics , vol.38 , Issue.3 , pp. 310-326
    • Denessiouk, K.A.1    Johnson, M.S.2
  • 23
    • 0032564590 scopus 로고    scopus 로고
    • Rational design of an inhibitor of dethiobiotin synthetase; interaction of 6-hydroxypyrimidin-4(3H)-one with the adenine base binding site
    • PII S0040402098009995
    • Alexeev D, Baxter RL, Campopiano DJ, McAlpine RS, McIver L, &, Sawyer L, (1998) Rational design of an inhibitor of dethiobiotin synthetase; interaction of 6-hydroxypyrimidin-4(3H)-one with the adenine base binding site. Tetrahedron 54, 15891-15898. (Pubitemid 28551912)
    • (1998) Tetrahedron , vol.54 , Issue.52 , pp. 15891-15898
    • Alexeev, D.1    Baxter, R.L.2    Campopiano, D.J.3    McAlpine, R.S.4    McIver, L.5    Sawyer, L.6
  • 25
    • 36749034218 scopus 로고    scopus 로고
    • In situ proteolysis for protein crystallization and structure determination
    • Midwest Center for Structural Genomics & Structural Genomics Consortium
    • Dong AP, Xu XH, Edward AM, & Midwest Center for Structural Genomics & Structural Genomics Consortium (2007) In situ proteolysis for protein crystallization and structure determination. Nat Methods 4, 1019-1021.
    • (2007) Nat Methods , vol.4 , pp. 1019-1021
    • Dong, A.P.1    Xu, X.H.2    Edward, A.M.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • DOI 10.1107/S0907444906019949
    • Minor W, Cymborowski M, Otwinowski Z, &, Chruszcz M, (2006) HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr D 62, 859-866. (Pubitemid 44125661)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.8 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 31
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64, 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 32
    • 0002634621 scopus 로고
    • Isomorphous replacement and anomalous scattering
    • SERC Daresbury Laboratory, Warrington, U.K
    • Otwinowski Z, (1991) Isomorphous replacement and anomalous scattering. Paper presented at the Daresbury Study Weekend Proceedings, SERC Daresbury Laboratory, Warrington, U.K.
    • (1991) Daresbury Study Weekend Proceedings
    • Otwinowski, Z.1
  • 33
    • 0000449646 scopus 로고
    • Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • Cowtan KD, &, Main P, (1993) Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints. Acta Crystallogr D 49, 148-157.
    • (1993) Acta Crystallogr D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 34
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • DOI 10.1038/8263
    • Perrakis A, Morris R, &, Lamzin VS, (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6, 458-463. (Pubitemid 29218016)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 37
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification, and model building
    • DOI 10.1107/S0909049503023938
    • Terwilliger T, (2004) SOLVE and RESOLVE: automated structure solution, density modification, and model building. J Synchrotron Radiat 11, 49-52. (Pubitemid 40085632)
    • (2004) Journal of Synchrotron Radiation , vol.11 , Issue.1 , pp. 49-52
    • Terwilliger, T.1
  • 40
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, &, Teplyakov A, (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30, 1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 41
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, &, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D 62, 439-450.
    • (2006) Acta Crystallogr D , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 42
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J, &, Merritt EA, (2006) TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr 39, 109-111.
    • (2006) J Appl Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 45
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, &, Park J, (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16, 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 46
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel E, &, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D 60, 2256-2268. (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 48
    • 48449087960 scopus 로고    scopus 로고
    • PROMALS3D web server for accurate multiple protein sequence and structure alignments
    • Pei JM, Tang M, &, Grishin NV, (2008) PROMALS3D web server for accurate multiple protein sequence and structure alignments. Nucleic Acids Res 36, W30-W34.
    • (2008) Nucleic Acids Res , vol.36
    • Pei, J.M.1    Tang, M.2    Grishin, N.V.3
  • 49
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • DOI 10.1093/nar/gkn072
    • Pei JM, Kim BH, &, Grishin NV, (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36, 2295-2300. (Pubitemid 351567002)
    • (2008) Nucleic Acids Research , vol.36 , Issue.7 , pp. 2295-2300
    • Pei, J.1    Kim, B.-H.2    Grishin, N.V.3
  • 50
    • 0034843597 scopus 로고    scopus 로고
    • AL2CO: Calculation of positional conservation in a protein sequence alignment
    • Pei JM, &, Grishin NV, (2001) AL2CO: calculation of positional conservation in a protein sequence alignment. Bioinformatics 17, 700-712. (Pubitemid 32851378)
    • (2001) Bioinformatics , vol.17 , Issue.8 , pp. 700-712
    • Pei, J.1    Grishin, N.V.2
  • 51
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson EG, &, Thornton JM, (1996) PROMOTIF-Aaprogram to identify and analyze structural motifs in proteins. Protein Sci 5, 212-220. (Pubitemid 26054277)
    • (1996) Protein Science , vol.5 , Issue.2 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2


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