메뉴 건너뛰기




Volumn 339, Issue 2, 2004, Pages 265-278

Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis

Author keywords

Bacillus subtilis; GTP; GTP binding protein; GTPase; TRAFAC, translation factor related; YsxC

Indexed keywords

ANTIINFECTIVE AGENT; ASPARTIC ACID; BACTERIAL PROTEIN; CATION; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATASE; MAGNESIUM ION; NUCLEOTIDE; PROTEIN YSXC; UNCLASSIFIED DRUG;

EID: 2342580711     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.043     Document Type: Article
Times cited : (33)

References (53)
  • 1
    • 0034909325 scopus 로고    scopus 로고
    • Evolution of a molecular switch: Universal bacterial GTPases regulate ribosome function
    • Caldon C.E., Yoong P., March P.E. Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function. Mol. Microbiol. 41:2001;289-297
    • (2001) Mol. Microbiol. , vol.41 , pp. 289-297
    • Caldon, C.E.1    Yoong, P.2    March, P.E.3
  • 2
    • 0038352105 scopus 로고    scopus 로고
    • Function of the universally conserved bacterial GTPases
    • Caldon C.E., March P.E. Function of the universally conserved bacterial GTPases. Curr. Opin. Microbiol. 6:2003;135-139
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 135-139
    • Caldon, C.E.1    March, P.E.2
  • 3
    • 0034460090 scopus 로고    scopus 로고
    • YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168
    • Prágai Z., Harwood C.R. YsxC, a putative GTP-binding protein essential for growth of Bacillus subtilis 168. J. Bacteriol. 182:2000;6819-6823
    • (2000) J. Bacteriol. , vol.182 , pp. 6819-6823
    • Prágai, Z.1    Harwood, C.R.2
  • 4
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317:2002;41-72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 5
    • 0036855348 scopus 로고    scopus 로고
    • Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis
    • Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S., Ogasawara N. Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis. Microbiology. 148:2002;3539-3552
    • (2002) Microbiology , vol.148 , pp. 3539-3552
    • Morimoto, T.1    Loh, P.C.2    Hirai, T.3    Asai, K.4    Kobayashi, K.5    Moriya, S.6    Ogasawara, N.7
  • 9
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang S. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66:1997;639-678
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.1
  • 10
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter I.R., Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science. 294:2001;1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 11
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:1991;117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 13
    • 2342666190 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding protein, YsxC, from Bacillus subtilis
    • Das S.K., Sedelnikova S.E., Baker P.J., Ruzheinikov S.N., Foster S.J., Rice D.W. Expression, purification, crystallization and preliminary crystallographic analysis of a putative GTP-binding protein, YsxC, from Bacillus subtilis. Acta Crystallog. sect. D. 60:2004;166-168
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 166-168
    • Das, S.K.1    Sedelnikova, S.E.2    Baker, P.J.3    Ruzheinikov, S.N.4    Foster, S.J.5    Rice, D.W.6
  • 14
    • 0033571343 scopus 로고    scopus 로고
    • ras in complex with GTP: New insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins
    • ras in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure. 7:1999;1311-1324
    • (1999) Structure , vol.7 , pp. 1311-1324
    • Scheidig, A.J.1    Burmester, C.2    Goody, R.S.3
  • 15
    • 0033587699 scopus 로고    scopus 로고
    • Crystal structure of ERA: A GTPase-dependent cell cycle regulator containing an RNA binding motif
    • Chen X., Court D.L., Ji X. Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. Proc. Natl Acad. Sci. USA. 96:1999;8396-8401
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8396-8401
    • Chen, X.1    Court, D.L.2    Ji, X.3
  • 16
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • Buglino J., Dhen V., Hakimian P., Lima C.D. Structural and biochemical analysis of the Obg GTP binding protein. Structure. 10:2002;1581-1592
    • (2002) Structure , vol.10 , pp. 1581-1592
    • Buglino, J.1    Dhen, V.2    Hakimian, P.3    Lima, C.D.4
  • 17
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution
    • Song H., Parsons M.R., Rowsell S., Leonard G., Phillips S.E.V. Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 Å resolution. J. Mol. Biol. 285:1999;1245-1256
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.V.5
  • 19
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • Prakash B., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 403:2000;567-571
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 20
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • Freymann D.M., Keenan R.J., Stroud R.M., Walter P. Structure of the conserved GTPase domain of the signal recognition particle. Nature. 385:1997;361-364
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 21
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å Nature. 409:2001;1071-1077
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5    Sigler, P.B.6
  • 22
    • 0032514722 scopus 로고    scopus 로고
    • 2+: A crystallographic titration experiment
    • 2+: a crystallographic titration experiment. Biochemistry. 37:1998;14376-14385
    • (1998) Biochemistry , vol.37 , pp. 14376-14385
    • Coleman, D.E.1    Sprang, S.R.2
  • 24
    • 0029831063 scopus 로고    scopus 로고
    • Kinetics of interactions of Rab5 and Rab7 with nucleotides and magnesium ions
    • Simon I., Zerial M., Goody R.S. Kinetics of interactions of Rab5 and Rab7 with nucleotides and magnesium ions. J. Biol. Chem. 271:1996;20470-20478
    • (1996) J. Biol. Chem. , vol.271 , pp. 20470-20478
    • Simon, I.1    Zerial, M.2    Goody, R.S.3
  • 25
    • 0025218124 scopus 로고
    • Guanine nucleotide binding properties of the mammalian RalA protein produced in Escherichia coli
    • Frech M., Schlichting I., Wittinghofer A., Chardin P. Guanine nucleotide binding properties of the mammalian RalA protein produced in Escherichia coli. J. Biol. Chem. 265:1990;6353-6359
    • (1990) J. Biol. Chem. , vol.265 , pp. 6353-6359
    • Frech, M.1    Schlichting, I.2    Wittinghofer, A.3    Chardin, P.4
  • 26
    • 0027967593 scopus 로고
    • A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures
    • Artymiuk P.J., Poirrette A.R., Grindley H.M., Rice D.W., Willett P. A graph-theoretic approach to the identification of three-dimensional patterns of amino acid side-chains in protein structures. J. Mol. Biol. 243:1994;327-344
    • (1994) J. Mol. Biol. , vol.243 , pp. 327-344
    • Artymiuk, P.J.1    Poirrette, A.R.2    Grindley, H.M.3    Rice, D.W.4    Willett, P.5
  • 27
    • 0023887507 scopus 로고
    • The Escherichia coli Ras-like protein (Era) has GTPase activity and is essential for cell growth
    • March P.E., Lerner C.G., Ahnn J., Cui X., Inouye M. The Escherichia coli Ras-like protein (Era) has GTPase activity and is essential for cell growth. Oncogene. 2:1988;539-544
    • (1988) Oncogene , vol.2 , pp. 539-544
    • March, P.E.1    Lerner, C.G.2    Ahnn, J.3    Cui, X.4    Inouye, M.5
  • 28
    • 0025904269 scopus 로고
    • A GTP-binding protein (Era) has an essential role in growth rate and cell cycle control in Escherichia coli
    • Gollop N., March P.E. A GTP-binding protein (Era) has an essential role in growth rate and cell cycle control in Escherichia coli. J. Bacteriol. 173:1991;2265-2270
    • (1991) J. Bacteriol. , vol.173 , pp. 2265-2270
    • Gollop, N.1    March, P.E.2
  • 29
    • 0031953140 scopus 로고    scopus 로고
    • Cell cycle arrest in Era GTPase mutants: A potential growth rate-regulated checkpoint in Escherichia coli
    • Britton R.A., Powell B.S., Dasgupta S., Sun Q., Margolin W., Lupski J.R., Court D.L. Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated checkpoint in Escherichia coli. Mol. Microbiol. 27:1998;739-750
    • (1998) Mol. Microbiol. , vol.27 , pp. 739-750
    • Britton, R.A.1    Powell, B.S.2    Dasgupta, S.3    Sun, Q.4    Margolin, W.5    Lupski, J.R.6    Court, D.L.7
  • 30
    • 0032857928 scopus 로고    scopus 로고
    • 16S rRNA is bound to era of Streptococcus pneumoniae
    • Meier T.I., Peery R.B., Jaskunas S.R., Zhao G. 16S rRNA is bound to era of Streptococcus pneumoniae. J. Bacteriol. 181:1999;5242-5249
    • (1999) J. Bacteriol. , vol.181 , pp. 5242-5249
    • Meier, T.I.1    Peery, R.B.2    Jaskunas, S.R.3    Zhao, G.4
  • 31
    • 0032846245 scopus 로고    scopus 로고
    • The widely conserved Era G-protein contains an RNA-binding domain required for Era function in vivo
    • Johnstone B.H., Handler A.A., Chao D.K., Nguyen V., Smith M., Ryu S.Y., et al. The widely conserved Era G-protein contains an RNA-binding domain required for Era function in vivo. Mol. Microbiol. 33:1999;1118-1131
    • (1999) Mol. Microbiol. , vol.33 , pp. 1118-1131
    • Johnstone, B.H.1    Handler, A.A.2    Chao, D.K.3    Nguyen, V.4    Smith, M.5    Ryu, S.Y.6
  • 32
    • 0032752483 scopus 로고    scopus 로고
    • A new essential gene of the minimal genome affecting cell division
    • Dassain M., Leroy A., Colosetti L., Carolé S., Bouché J.-P. A new essential gene of the minimal genome affecting cell division. Biochimie. 81:1999;889-895
    • (1999) Biochimie , vol.81 , pp. 889-895
    • Dassain, M.1    Leroy, A.2    Colosetti, L.3    Carolé, S.4    Bouché, J.-P.5
  • 33
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 348:1990;125-132
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 34
    • 0035663042 scopus 로고    scopus 로고
    • Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase
    • Kurimoto K., Fukai S., Nureki O., Muto Y., Yokoyama S. Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase. Structure. 9:2001;1253-1263
    • (2001) Structure , vol.9 , pp. 1253-1263
    • Kurimoto, K.1    Fukai, S.2    Nureki, O.3    Muto, Y.4    Yokoyama, S.5
  • 35
    • 0032765908 scopus 로고    scopus 로고
    • Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma(B)
    • Scott J.M., Haldenwang W.G. Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor sigma(B). J. Bacteriol. 181:1999;4653-4660
    • (1999) J. Bacteriol. , vol.181 , pp. 4653-4660
    • Scott, J.M.1    Haldenwang, W.G.2
  • 36
    • 0031685531 scopus 로고    scopus 로고
    • An essential GTP-binding protein functions as a regulator for differentiation in Streptomyces coelicolor
    • Okamoto S., Ochi K. An essential GTP-binding protein functions as a regulator for differentiation in Streptomyces coelicolor. Mol. Microbiol. 30:1998;107-119
    • (1998) Mol. Microbiol. , vol.30 , pp. 107-119
    • Okamoto, S.1    Ochi, K.2
  • 37
    • 0025876511 scopus 로고
    • Pleiotropic changes resulting from depletion of Era, an essential GTP-binding protein in Escherichia coli
    • Lerner C.G., Inouye M. Pleiotropic changes resulting from depletion of Era, an essential GTP-binding protein in Escherichia coli. Mol. Microbiol. 5:1991;951-957
    • (1991) Mol. Microbiol. , vol.5 , pp. 951-957
    • Lerner, C.G.1    Inouye, M.2
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4. 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
  • 42
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters in isomorphous replacement and anomalous scattering
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington, UK: Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters in isomorphous replacement and anomalous scattering. Wolf W., Evans P.R., Leslie A.G.W. Proceedings of the CCP4 Study Weekend. 1991;80-86 Daresbury Laboratory, Warrington, UK
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-86
    • Otwinowski, Z.1
  • 43
    • 0002583957 scopus 로고
    • 'dm' an automated procedure for phase improvements by density modification
    • Cowtan K. 'dm' an automated procedure for phase improvements by density modification. Joint CCP4 and ESF-EACBM Newsletter Protein Crystallog. 31:1994;34-38
    • (1994) Joint CCP4 and ESF-EACBM Newsletter Protein Crystallog. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 45
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 46
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang J.-S., Brünger A.T. Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243:1994;100-115
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 47
    • 0001696252 scopus 로고    scopus 로고
    • Correlation of internal torsional motion with overall molecular motion in crystals
    • Schomaker V., Trueblood K.N. Correlation of internal torsional motion with overall molecular motion in crystals. Acta Crystallog. sect. B. 54:1998;507-514
    • (1998) Acta Crystallog. Sect. B , vol.54 , pp. 507-514
    • Schomaker, V.1    Trueblood, K.N.2
  • 48
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallog. sect. D. 57:2001;122-133
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 49
    • 0036223442 scopus 로고    scopus 로고
    • Homo crystallographicus - Quo vadis?
    • Kleywegt G.J., Jones T.A. Homo crystallographicus - quo vadis? Structure. 10:2002;465-472
    • (2002) Structure , vol.10 , pp. 465-472
    • Kleywegt, G.J.1    Jones, T.A.2
  • 53
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex N., Peitsch M.C. SWISS-MODEL and Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis. 18:1997;2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.