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Volumn 49, Issue 41, 2010, Pages 8929-8936

HMP binding protein ThiY and HMP-P synthase THI5 are structural homologues

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BACTERIOLOGY; BINDING ENERGY; BIOLOGICAL MEMBRANES; BIOSYNTHESIS; METHANOL; PROTEINS; YEAST;

EID: 77957891495     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101209t     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 33748920368 scopus 로고    scopus 로고
    • Thiamine (vitamin B1) deficiency and associated brain damage is still common throughout the world and prevention is simple and safe!
    • Harper, C. (2006) Thiamine (vitamin B1) deficiency and associated brain damage is still common throughout the world and prevention is simple and safe! Eur. J. Neurol. 13, 1078-1082
    • (2006) Eur. J. Neurol. , vol.13 , pp. 1078-1082
    • Harper, C.1
  • 2
    • 0030162658 scopus 로고    scopus 로고
    • The biosynthesis and degradation of thiamin (vitamin B1)
    • Begley, T. (1996) The biosynthesis and degradation of thiamin (vitamin B1) Nat. Prod. Rep. 13, 177-185
    • (1996) Nat. Prod. Rep. , vol.13 , pp. 177-185
    • Begley, T.1
  • 3
    • 0346850972 scopus 로고    scopus 로고
    • Structural biology of enzymes of the thiamin biosynthesis pathway
    • Settembre, E., Begley, T. P., and Ealick, S. E. (2003) Structural biology of enzymes of the thiamin biosynthesis pathway Curr. Opin. Struct. Biol. 13, 739-747
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 739-747
    • Settembre, E.1    Begley, T.P.2    Ealick, S.E.3
  • 5
    • 33748803376 scopus 로고    scopus 로고
    • Structural Insights into the Function of the Thiamin Biosynthetic Enzyme Thi4 from Saccharomyces cerevisiae
    • Jurgenson, C. T., Chatterjee, A., Begley, T. P., and Ealick, S. E. (2006) Structural Insights into the Function of the Thiamin Biosynthetic Enzyme Thi4 from Saccharomyces cerevisiae Biochemistry 45, 11061-11070
    • (2006) Biochemistry , vol.45 , pp. 11061-11070
    • Jurgenson, C.T.1    Chatterjee, A.2    Begley, T.P.3    Ealick, S.E.4
  • 6
    • 50249154198 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin-thiazole in eukaryotes: Identification of a thiazole tautomer intermediate
    • Chatterjee, A., Schroeder, F. C., Jurgenson, C. T., Ealick, S. E., and Begley, T. P. (2008) Biosynthesis of the thiamin-thiazole in eukaryotes: Identification of a thiazole tautomer intermediate J. Am. Chem. Soc. 130, 11394-11398
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11394-11398
    • Chatterjee, A.1    Schroeder, F.C.2    Jurgenson, C.T.3    Ealick, S.E.4    Begley, T.P.5
  • 7
    • 0037804259 scopus 로고    scopus 로고
    • The THI5 gene family of Saccharomyces cerevisiae: Distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine
    • Wightman, R. and Meacock, P. A. (2003) The THI5 gene family of Saccharomyces cerevisiae: Distribution of homologues among the hemiascomycetes and functional redundancy in the aerobic biosynthesis of thiamin from pyridoxine Microbiology 149, 1447-1460
    • (2003) Microbiology , vol.149 , pp. 1447-1460
    • Wightman, R.1    Meacock, P.A.2
  • 8
    • 0142183433 scopus 로고    scopus 로고
    • Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid
    • Zeidler, J., Sayer, B. G., and Spenser, I. D. (2003) Biosynthesis of vitamin B1 in yeast. Derivation of the pyrimidine unit from pyridoxine and histidine. Intermediacy of urocanic acid J. Am. Chem. Soc. 125, 13094-13105
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13094-13105
    • Zeidler, J.1    Sayer, B.G.2    Spenser, I.D.3
  • 9
    • 33747108569 scopus 로고    scopus 로고
    • Recent progress in understanding thiamin biosynthesis and its genetic regulation in Saccharomyces cerevisiae
    • Nosaka, K. (2006) Recent progress in understanding thiamin biosynthesis and its genetic regulation in Saccharomyces cerevisiae Appl. Microbiol. Biotechnol. 72, 30-40
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 30-40
    • Nosaka, K.1
  • 10
    • 2242446202 scopus 로고    scopus 로고
    • Comparative Genomics of Thiamin Biosynthesis in Procaryotes. New genes and regulatory mechanisms
    • Rodionov, D. A., Vitreschak, A. G., Mironov, A. A., and Gelfand, M. S. (2002) Comparative Genomics of Thiamin Biosynthesis in Procaryotes. New genes and regulatory mechanisms J. Biol. Chem. 277, 48949-48959
    • (2002) J. Biol. Chem. , vol.277 , pp. 48949-48959
    • Rodionov, D.A.1    Vitreschak, A.G.2    Mironov, A.A.3    Gelfand, M.S.4
  • 11
    • 0036411929 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the periplasmic space thiamin-binding protein of the thiamin traffic ATPase in Escherichia coli
    • Hollenbach, A. D., Dickson, K. A., and Washabaugh, M. W. (2002) Overexpression, purification, and characterization of the periplasmic space thiamin-binding protein of the thiamin traffic ATPase in Escherichia coli Protein Expression Purif. 25, 508-518
    • (2002) Protein Expression Purif. , vol.25 , pp. 508-518
    • Hollenbach, A.D.1    Dickson, K.A.2    Washabaugh, M.W.3
  • 12
    • 0032502743 scopus 로고    scopus 로고
    • ThiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphae in Salmonella typhimurium
    • Webb, E., Claas, K., and Downs, D. (1998) thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphae in Salmonella typhimurium J. Biol. Chem. 273, 8946-8950
    • (1998) J. Biol. Chem. , vol.273 , pp. 8946-8950
    • Webb, E.1    Claas, K.2    Downs, D.3
  • 13
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P. M. and George, A. M. (2004) The ABC transporter structure and mechanism: Perspectives on recent research Cell. Mol. Life Sci. 61, 682-699
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 14
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L. and Chen, J. (2004) ATP-binding cassette transporters in bacteria Annu. Rev. Biochem. 73, 241-268
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 15
    • 38849178185 scopus 로고    scopus 로고
    • Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor
    • Soriano, E. V., Rajashankar, K. R., Hanes, J. W., Bale, S., Begley, T. P., and Ealick, S. E. (2008) Structural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestor Biochemistry 47, 1346-1357
    • (2008) Biochemistry , vol.47 , pp. 1346-1357
    • Soriano, E.V.1    Rajashankar, K.R.2    Hanes, J.W.3    Bale, S.4    Begley, T.P.5    Ealick, S.E.6
  • 16
    • 0015611501 scopus 로고
    • Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane
    • Hantke, K. and Braun, V. (1973) Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane Eur. J. Biochem. 34, 284-296
    • (1973) Eur. J. Biochem. , vol.34 , pp. 284-296
    • Hantke, K.1    Braun, V.2
  • 17
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran, K. and Wu, H. C. (1994) Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol J. Biol. Chem. 269, 19701-19706
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. (2008) A short history of SHELX Acta Crystallogr. A64, 112-122
    • (2008) Acta Crystallogr. , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 21
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for phasing with SHELX programs
    • Pape, T. and Schneider, T. R. (2004) HKL2MAP: A graphical user interface for phasing with SHELX programs J. Appl. Crystallogr. 37, 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 24
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 ()
    • Collaborative Computational Project Number 4 (1994) The CCP4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 25
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. and Berendzen, J. (1999) Automated MAD and MIR structure solution Acta Crystallogr. D55, 849-861
    • (1999) Acta Crystallogr. , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 26
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • Kleywegt, G. J. and Jones, T. A. (1998) Databases in protein crystallography Acta Crystallogr. D54, 1119-1131
    • (1998) Acta Crystallogr. , vol.54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2
  • 29
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S. J. and Kollman, P. A. (1986) An all atom force field for simulations of proteins and nucleic acids J. Comput. Chem. 7, 230-252
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2
  • 34
    • 84988112508 scopus 로고
    • An Efficient Newton-like Method for Molecular Mechanics Energy Minimization of Large Molecules
    • Ponder, J. W. and Richards, F. M. (1987) An Efficient Newton-like Method for Molecular Mechanics Energy Minimization of Large Molecules J. Comput. Chem. 8, 1016-1024
    • (1987) J. Comput. Chem. , vol.8 , pp. 1016-1024
    • Ponder, J.W.1    Richards, F.M.2
  • 35
  • 36
    • 66149116873 scopus 로고    scopus 로고
    • Trapping open and closed forms of FitE-A group III periplasmic binding protein
    • Shi, R., Proteau, A., Wagner, J., Cui, Q., Purisima, E. O., Matte, A., and Cygler, M. (2009) Trapping open and closed forms of FitE-A group III periplasmic binding protein Proteins 75, 598-609
    • (2009) Proteins , vol.75 , pp. 598-609
    • Shi, R.1    Proteau, A.2    Wagner, J.3    Cui, Q.4    Purisima, E.O.5    Matte, A.6    Cygler, M.7
  • 37
    • 0033548125 scopus 로고    scopus 로고
    • Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history
    • Fukami-Kobayashi, K., Tateno, Y., and Nishikawa, K. (1999) Domain dislocation: A change of core structure in periplasmic binding proteins in their evolutionary history J. Mol. Biol. 286, 279-290
    • (1999) J. Mol. Biol. , vol.286 , pp. 279-290
    • Fukami-Kobayashi, K.1    Tateno, Y.2    Nishikawa, K.3
  • 38
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3 Bioinformatics 24, 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 39
    • 77950828672 scopus 로고    scopus 로고
    • Structure of the aliphatic sulfonate-binding protein SsuA from Escherichia coli
    • Beale, J., Lee, S. Y., Iwata, S., and Beis, K. (2010) Structure of the aliphatic sulfonate-binding protein SsuA from Escherichia coli Acta Crystallogr. F66, 391-396
    • (2010) Acta Crystallogr. , vol.66 , pp. 391-396
    • Beale, J.1    Lee, S.Y.2    Iwata, S.3    Beis, K.4
  • 40
    • 33745615124 scopus 로고    scopus 로고
    • Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity
    • Koropatkin, N. M., Pakrasi, H. B., and Smith, T. J. (2006) Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity Proc. Natl. Acad. Sci. U.S.A. 103, 9820-9825
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9820-9825
    • Koropatkin, N.M.1    Pakrasi, H.B.2    Smith, T.J.3
  • 41
    • 34047266662 scopus 로고    scopus 로고
    • The structure of a cyanobacterial bicarbonate transport protein, CmpA
    • Koropatkin, N. M., Koppenaal, D. W., Pakrasi, H. B., and Smith, T. J. (2007) The structure of a cyanobacterial bicarbonate transport protein, CmpA J. Biol. Chem. 282, 2606-2614
    • (2007) J. Biol. Chem. , vol.282 , pp. 2606-2614
    • Koropatkin, N.M.1    Koppenaal, D.W.2    Pakrasi, H.B.3    Smith, T.J.4
  • 44
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Ever-expanding roles
    • Fontecave, M. (2006) Iron-sulfur clusters: Ever-expanding roles Nat. Chem. Biol. 2, 171-174
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 45
    • 53849132731 scopus 로고    scopus 로고
    • Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes
    • Saunders, A. H., Griffiths, A. E., Lee, K. H., Cicchillo, R. M., Tu, L., Stromberg, J. A., Krebs, C., and Booker, S. J. (2008) Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes Biochemistry 47, 10999-11012
    • (2008) Biochemistry , vol.47 , pp. 10999-11012
    • Saunders, A.H.1    Griffiths, A.E.2    Lee, K.H.3    Cicchillo, R.M.4    Tu, L.5    Stromberg, J.A.6    Krebs, C.7    Booker, S.J.8
  • 46
    • 0032506058 scopus 로고    scopus 로고
    • Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 Å resolution
    • Campobasso, N., Costello, C. A., Kinsland, C., Begley, T. P., and Ealick, S. E. (1998) Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 Å resolution Biochemistry 37, 15981-15989
    • (1998) Biochemistry , vol.37 , pp. 15981-15989
    • Campobasso, N.1    Costello, C.A.2    Kinsland, C.3    Begley, T.P.4    Ealick, S.E.5


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