메뉴 건너뛰기




Volumn 44, Issue 42, 2005, Pages 13962-13969

SAS solution structures of the Apo and Mg2+/BeF3 --bound receiver domain of DctD from Sinorhizobium meliloti

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL LATTICES; DIMERS; MAGNESIUM COMPOUNDS; PROTEINS;

EID: 27144479211     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051129u     Document Type: Article
Times cited : (10)

References (32)
  • 3
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains
    • Lee, S. Y., DeLaTorre, A., Yan, D., Kustu, S., Nixon, B. T., and Wemmer, D. E. (2003) Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains, Genes Dev. 17, 2552-2563.
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1    DeLaTorre, A.2    Yan, D.3    Kustu, S.4    Nixon, B.T.5    Wemmer, D.E.6
  • 4
    • 0021678529 scopus 로고
    • Molecular cloning and genetic organization of C4-dicarboxylate transport genes from Rhizobium leguminosarum
    • Ronson, C. W., Astwood, P. M., and Downie, A. J. (1984) Molecular cloning and genetic organization of C4-dicarboxylate transport genes from Rhizobium leguminosarum, J. Bacteriol. 160, 903-909.
    • (1984) J. Bacteriol. , vol.160 , pp. 903-909
    • Ronson, C.W.1    Astwood, P.M.2    Downie, A.J.3
  • 5
    • 0020645150 scopus 로고
    • Symbiotic properties of C4-dicarboxylate acid transport mutants of Rhizobium leguminosarum
    • Finan, T. M., Wood, J. M., and Jordan, D. C. (1983) Symbiotic properties of C4-dicarboxylate acid transport mutants of Rhizobium leguminosarum, J. Bacteriol. 154, 1403-1413.
    • (1983) J. Bacteriol. , vol.154 , pp. 1403-1413
    • Finan, T.M.1    Wood, J.M.2    Jordan, D.C.3
  • 6
    • 0023652071 scopus 로고
    • Deduced products of C4-dicarboxylate transport regulatory genes of Rhizobium leguminosarum are homologous to nitrogen regulatory gene products
    • Ronson, C. W., Astwood, P. M., Nixon, B. T., and Ausubel, F. M. (1987) Deduced products of C4-dicarboxylate transport regulatory genes of Rhizobium leguminosarum are homologous to nitrogen regulatory gene products, Nucleic Acids Res. 15, 7921-7934.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 7921-7934
    • Ronson, C.W.1    Astwood, P.M.2    Nixon, B.T.3    Ausubel, F.M.4
  • 9
    • 0036712106 scopus 로고    scopus 로고
    • Biochemical evidence for multiple dimeric states of the Sinorhizobium meliloti DctD receiver domain
    • Park, S., Zhang, H., Jones, A. D., and Nixon, B. T. (2002) Biochemical evidence for multiple dimeric states of the Sinorhizobium meliloti DctD receiver domain, Biochemistry 41, 10934-10941.
    • (2002) Biochemistry , vol.41 , pp. 10934-10941
    • Park, S.1    Zhang, H.2    Jones, A.D.3    Nixon, B.T.4
  • 12
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 13
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules, Methods Mol. Biol. 278, 313-352.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 14
    • 0035443198 scopus 로고    scopus 로고
    • Biophysical studies by ultracentrifugation
    • Laue, T. (2001) Biophysical studies by ultracentrifugation, Curr. Opin. Struct. Biol. 11, 579-583.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 579-583
    • Laue, T.1
  • 15
    • 0542443295 scopus 로고    scopus 로고
    • The 30m small-angle neutron scattering instruments at the National Institute of Standards and Technology
    • Glinka, C. J., Barker, J. B., Hammouda, B., Krueger, S., Moyer, J. J., and Orts, W. J. (1998) The 30m Small-Angle Neutron Scattering Instruments at the National Institute of Standards and Technology, J. Appl. Crystallogr. 31, 430-445.
    • (1998) J. Appl. Crystallogr. , vol.31 , pp. 430-445
    • Glinka, C.J.1    Barker, J.B.2    Hammouda, B.3    Krueger, S.4    Moyer, J.J.5    Orts, W.J.6
  • 17
    • 0141571313 scopus 로고    scopus 로고
    • High-resolution wide-angle X-ray scattering of protein solutions: Effect of beam dose on protein integrity
    • Fischetti, R. F., Rodi, D. J., Mirza, A., Irving, T. C., Kondrashkina, E., and Makowski, L. (2003) High-resolution wide-angle X-ray scattering of protein solutions: Effect of beam dose on protein integrity, J. Synchrotron Radiat. 10, 398-404.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 398-404
    • Fischetti, R.F.1    Rodi, D.J.2    Mirza, A.3    Irving, T.C.4    Kondrashkina, E.5    Makowski, L.6
  • 21
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 22
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys. J. 76, 2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 23
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. J. (2001) Determination of domain structure of proteins from X-ray solution scattering, Biophys. J. 80, 2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 25
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C., and Koch, M. H. J. (1995) CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates, J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 26
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA: A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • Konarev, P. V., Petoukhov, M. V., and Svergun, D. I. (2001) MASSHA: A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data, J. Appl. Crystallogr. 34, 527-532.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 28
    • 11844264877 scopus 로고    scopus 로고
    • Radiation damage to a protein solution, detection by synchrotron X-ray small-angle scattering: Dose-related considerations and suppression by cryoprotectants
    • Kuwamoto, S., Akiyama, S., and Fujisawa, T. (2004) Radiation damage to a protein solution, detection by synchrotron X-ray small-angle scattering: Dose-related considerations and suppression by cryoprotectants, J. Synchrotron Radiat. 11, 462-468.
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 462-468
    • Kuwamoto, S.1    Akiyama, S.2    Fujisawa, T.3
  • 29
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and Svergun, D. I. (2000) Automated matching of high- and low-resolution structural models, J. Appl. Crystallogr. 34, 33-41.
    • (2000) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 30
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering, J. Appl. Crystallogr. 36, 860-864.
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 31
    • 0347383756 scopus 로고    scopus 로고
    • Looking behind the beamstop: X-ray solution scattering studies of structure and conformational changes of biological macromolecules
    • Vachette, P., Koch, M. H., and Svergun, D. I. (2003) Looking behind the beamstop: X-ray solution scattering studies of structure and conformational changes of biological macromolecules, Methods Enzymol. 374, 584-615.
    • (2003) Methods Enzymol. , vol.374 , pp. 584-615
    • Vachette, P.1    Koch, M.H.2    Svergun, D.I.3
  • 32
    • 25144472529 scopus 로고    scopus 로고
    • Negative regulation of AAA+ ATPase assembly by two component receiver domains: A transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria
    • Published online September 14
    • Doucleff, M., Chen, B., Maris, A. E., Wemmer, D. E., Kondrashkina, E., and Nixon, B. T. (2005) Negative Regulation of AAA+ ATPase Assembly by Two Component Receiver Domains: A Transcription Activation Mechanism that is Conserved in Mesophilic and Extremely Hyperthermophilic Bacteria, J. Mol. Biol. Published online September 14.
    • (2005) J. Mol. Biol.
    • Doucleff, M.1    Chen, B.2    Maris, A.E.3    Wemmer, D.E.4    Kondrashkina, E.5    Nixon, B.T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.