메뉴 건너뛰기




Volumn 43, Issue 32, 2004, Pages 10343-10352

A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; DIMERS; HYDROPHILICITY; MATHEMATICAL MODELS; PROTEINS; STOICHIOMETRY;

EID: 4043110518     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0491292     Document Type: Article
Times cited : (26)

References (19)
  • 1
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
    • Anand, R., Hoskins, A. A., Stubbe, J., and Ealick, S. E. (2004) Domain Organization of Salmonella typhimurium Formylglycinamide Ribonucleotide Amidotransferase Revealed by X-ray Crystallography, Biochemistry 43, 10328-10342.
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 2
    • 4043093379 scopus 로고    scopus 로고
    • The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: An example of metabolite-mediated complex formation
    • Hoskins, A. A., Anand, R., Ealick, S. E., and Stubbe, J. (2004) The Formylglycinamide Ribonucleotide Amidotransferase Complex from Bacillus subtilis: An Example of Metabolite-Mediated Complex Formation, Biochemistry 43, 10314-10327.
    • (2004) Biochemistry , vol.43 , pp. 10314-10327
    • Hoskins, A.A.1    Anand, R.2    Ealick, S.E.3    Stubbe, J.4
  • 3
    • 0036836521 scopus 로고    scopus 로고
    • Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase
    • Batra, R., Christendat, D., Edwards, A., Arrowsmith, C., and Tong, L. (2002) Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase, Proteins 49, 285-288.
    • (2002) Proteins , vol.49 , pp. 285-288
    • Batra, R.1    Christendat, D.2    Edwards, A.3    Arrowsmith, C.4    Tong, L.5
  • 4
    • 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
  • 6
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for the building of protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 7
    • 0038325358 scopus 로고    scopus 로고
    • Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: Open-closed conformational change and ammonia tunneling
    • Omi, R., Mizuguchi, H., Goto, M., Miyahara, L, Hayashi, H., Kagamiyama, H., and Hirotsu, K. (2002) Structure of imidazole glycerol phosphate synthase from Thermus thermophilus HB8: open-closed conformational change and ammonia tunneling, J. Biochem (Toyko) 132, 759-765.
    • (2002) J. Biochem. (Toyko) , vol.132 , pp. 759-765
    • Omi, R.1    Mizuguchi, H.2    Goto, M.3    Miyahara, L.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7
  • 9
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 24, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 10
    • 50149097363 scopus 로고    scopus 로고
    • Comparative protein structure prediction
    • (Coligan, J. E., Ed.), John Wiley & Sons, Inc., New York. & Sons, Incorporated
    • Marti-Renom, M. A., Yerkovich, B., and Sali, A. (2002) Comparative protein structure prediction, in Current Protocols in Protein Science (Coligan, J. E., Ed.) pp 2.9.1-2.9.22, John Wiley & Sons, Inc., New York. & Sons, Incorporated.
    • (2002) Current Protocols in Protein Science
    • Marti-Renom, M.A.1    Yerkovich, B.2    Sali, A.3
  • 11
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints, J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 12
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L., and Sander, C. (1998) Touring protein fold space with Dali/FSSP, Nucleic Acids Res. 26, 316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 13
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical-method for the calculation of approximate born radii
    • Qiu, D., Shenkin, P. S., Hollinger, F. P., and Still, W. C. (1997) The GB/SA Continuum Model for Solvation. A Fast Analytical-Method for the Calculation of Approximate Born Radii, J. Phys. Chem. A 101, 3005-3014.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 16
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript which includes greatly enhanced colouring capabilities
    • Esnouf, R. (1997) An extensively modified version of Molscript which includes greatly enhanced colouring capabilities, J. Mol. Graphics 15, 132-134.
    • (1997) J. Mol. Graphics , vol.15 , pp. 132-134
    • Esnouf, R.1
  • 17
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R. M. (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps, Acta Crystallogr. D55, 938-940.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 938-940
    • Esnouf, R.M.1
  • 18
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 19
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic Molecular Graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.