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Volumn 385, Issue 1, 2009, Pages 51-64

The HupR Receiver Domain Crystal Structure in its Nonphospho and Inhibitory Phospho States

Author keywords

beryllium fluoride phosphorylation mimic; HupR; response regulator; X ray crystallography

Indexed keywords

HYDROGEN UPTAKE PROTEIN REGULATOR; NITROGEN REGULATORY PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 57749182194     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.027     Document Type: Article
Times cited : (14)

References (58)
  • 1
    • 0025881094 scopus 로고
    • Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis
    • Lukat G.S., Lee B.H., Mottonen J.M., Stock A.M., and Stock J.B. Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J. Biol. Chem. 266 (1991) 8348-8354
    • (1991) J. Biol. Chem. , vol.266 , pp. 8348-8354
    • Lukat, G.S.1    Lee, B.H.2    Mottonen, J.M.3    Stock, A.M.4    Stock, J.B.5
  • 2
    • 0032568513 scopus 로고    scopus 로고
    • A source of response regulator autophosphatase activity: the critical role of a residue adjacent to the SpoOF autophosphorylation active site
    • Zapf J., Madhusudan, Grimshaw C.E., Hoch J.A., Varughese K.I., and Whiteley J.M. A source of response regulator autophosphatase activity: the critical role of a residue adjacent to the SpoOF autophosphorylation active site. Biochemistry 37 (1998) 7725-7732
    • (1998) Biochemistry , vol.37 , pp. 7725-7732
    • Zapf, J.1    Madhusudan2    Grimshaw, C.E.3    Hoch, J.A.4    Varughese, K.I.5    Whiteley, J.M.6
  • 4
    • 0033456155 scopus 로고    scopus 로고
    • The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system
    • Dischert W., Vignais P.M., and Colbeau A. The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT/HupR system. Mol. Microbiol. 34 (1999) 995-1006
    • (1999) Mol. Microbiol. , vol.34 , pp. 995-1006
    • Dischert, W.1    Vignais, P.M.2    Colbeau, A.3
  • 5
    • 0026052331 scopus 로고
    • Identification and sequence analysis of the HupR1 gene, which encodes a response regulator of the NtrC family required for hydrogenase expression in Rhodobacter capsulatus
    • Richaud P., Colbeau A., Toussaint B., and Vignais P.M. Identification and sequence analysis of the HupR1 gene, which encodes a response regulator of the NtrC family required for hydrogenase expression in Rhodobacter capsulatus. J. Bacteriol. 173 (1991) 5928-5932
    • (1991) J. Bacteriol. , vol.173 , pp. 5928-5932
    • Richaud, P.1    Colbeau, A.2    Toussaint, B.3    Vignais, P.M.4
  • 7
    • 0037490143 scopus 로고    scopus 로고
    • Nucleotide-dependent triggering of RNA polymerase-DNA interactions by an AAA regulator of transcription
    • Cannon W., Bordes P., Wigneshweraraj S., and Buck M. Nucleotide-dependent triggering of RNA polymerase-DNA interactions by an AAA regulator of transcription. J. Biol. Chem. 278 (2003) 19815-19825
    • (2003) J. Biol. Chem. , vol.278 , pp. 19815-19825
    • Cannon, W.1    Bordes, P.2    Wigneshweraraj, S.3    Buck, M.4
  • 11
    • 0029166594 scopus 로고
    • The bacterial enhancer-binding protein NtrC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation
    • Wedel A., and Kustu S. The bacterial enhancer-binding protein NtrC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 9 (1995) 2042-2052
    • (1995) Genes Dev. , vol.9 , pp. 2042-2052
    • Wedel, A.1    Kustu, S.2
  • 12
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman C., Rombel I., North A.K., Bustamante C., and Kustu S. Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 275 (1997) 1658-1661
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5
  • 14
    • 0029016807 scopus 로고
    • Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain
    • Flashner Y., Weiss D.S., Keener J., and Kustu S. Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. J. Mol. Biol. 249 (1995) 700-713
    • (1995) J. Mol. Biol. , vol.249 , pp. 700-713
    • Flashner, Y.1    Weiss, D.S.2    Keener, J.3    Kustu, S.4
  • 15
    • 0033609111 scopus 로고    scopus 로고
    • Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC
    • Hwang I., Thorgeirsson T., Lee J., Kustu S., and Shin Y.K. Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC. Biochemistry 96 (1999) 4880-4885
    • (1999) Biochemistry , vol.96 , pp. 4880-4885
    • Hwang, I.1    Thorgeirsson, T.2    Lee, J.3    Kustu, S.4    Shin, Y.K.5
  • 16
    • 0033821317 scopus 로고    scopus 로고
    • Phosphorylation-induced signal propagation in the response regulator NtrC
    • Lee J., Owens J.T., Hwang I., Meares C., and Kustu S. Phosphorylation-induced signal propagation in the response regulator NtrC. J. Bacteriol. 182 (2000) 5188-5195
    • (2000) J. Bacteriol. , vol.182 , pp. 5188-5195
    • Lee, J.1    Owens, J.T.2    Hwang, I.3    Meares, C.4    Kustu, S.5
  • 18
    • 0033922187 scopus 로고    scopus 로고
    • Signaling through sigma
    • Gralla J.D. Signaling through sigma. Nat. Struct. Biol. 7 (2000) 530-532
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 530-532
    • Gralla, J.D.1
  • 19
    • 33646181238 scopus 로고    scopus 로고
    • Structural and functional studies of the response regulator HupR
    • Davies K.M., Skammaki V., Johnson L.N., and Venien-Bryan C. Structural and functional studies of the response regulator HupR. J. Mol. Biol. 359 (2006) 276-288
    • (2006) J. Mol. Biol. , vol.359 , pp. 276-288
    • Davies, K.M.1    Skammaki, V.2    Johnson, L.N.3    Venien-Bryan, C.4
  • 20
    • 0032525980 scopus 로고    scopus 로고
    • A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase
    • Bowman W.C., and Kranz R.G. A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase. Genes Dev. 12 (1998) 1884-1893
    • (1998) Genes Dev. , vol.12 , pp. 1884-1893
    • Bowman, W.C.1    Kranz, R.G.2
  • 21
    • 0032514688 scopus 로고    scopus 로고
    • A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus
    • Lenz O., and Friedrich B. A novel multicomponent regulatory system mediates H2 sensing in Alcaligenes eutrophus. Proc. Natl Acad. Sci. USA 95 (1998) 12474-12479
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12474-12479
    • Lenz, O.1    Friedrich, B.2
  • 22
    • 25144472529 scopus 로고    scopus 로고
    • + ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria
    • + ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria. J. Mol. Biol. 353 (2005) 242-255
    • (2005) J. Mol. Biol. , vol.353 , pp. 242-255
    • Doucleff, M.1    Chen, B.2    Maris, A.E.3    Wemmer, D.E.4    Kondrashkina, E.5    Nixon, B.T.6
  • 24
    • 0042165841 scopus 로고    scopus 로고
    • High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain
    • Hastings C.A., Lee S.Y., Cho H.S., Yan D., Kustu S., and Wemmer D.E. High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain. Biochemistry 42 (2003) 9081-9090
    • (2003) Biochemistry , vol.42 , pp. 9081-9090
    • Hastings, C.A.1    Lee, S.Y.2    Cho, H.S.3    Yan, D.4    Kustu, S.5    Wemmer, D.E.6
  • 27
    • 34547743126 scopus 로고    scopus 로고
    • Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride
    • Bachhawat P., and Stock A.M. Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride. J. Bacteriol. 189 (2007) 5987-5995
    • (2007) J. Bacteriol. , vol.189 , pp. 5987-5995
    • Bachhawat, P.1    Stock, A.M.2
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 29
    • 0342722461 scopus 로고    scopus 로고
    • Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid
    • Venien-Bryan C., Balavoine F., Toussaint B., Mioskowski C., Hewat E.A., Helme B., and Vignais P.M. Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid. J. Mol. Biol. 274 (1997) 687-692
    • (1997) J. Mol. Biol. , vol.274 , pp. 687-692
    • Venien-Bryan, C.1    Balavoine, F.2    Toussaint, B.3    Mioskowski, C.4    Hewat, E.A.5    Helme, B.6    Vignais, P.M.7
  • 32
    • 0025190798 scopus 로고
    • The function of isolated domains and chimeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae
    • Drummond M.H., Contreras A., and Mitchenall L.A. The function of isolated domains and chimeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae. Mol. Microbiol. 4 (1990) 29-37
    • (1990) Mol. Microbiol. , vol.4 , pp. 29-37
    • Drummond, M.H.1    Contreras, A.2    Mitchenall, L.A.3
  • 33
    • 0026070143 scopus 로고
    • The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription
    • Weiss D.S., Batut J., Klose K.E., Keener J., and Kustu S. The phosphorylated form of the enhancer-binding protein NtrC has an ATPase activity that is essential for activation of transcription. Cell 67 (1991) 155-167
    • (1991) Cell , vol.67 , pp. 155-167
    • Weiss, D.S.1    Batut, J.2    Klose, K.E.3    Keener, J.4    Kustu, S.5
  • 34
    • 33744780177 scopus 로고    scopus 로고
    • The structural basis for regulated assembly and function of the transcriptional activator NtrC
    • De Carlo S., Chen B., Hoover T.R., Kondrashkina E., Nogales E., and Nixon B.T. The structural basis for regulated assembly and function of the transcriptional activator NtrC. Genes Dev. 20 (2006) 1485-1495
    • (2006) Genes Dev. , vol.20 , pp. 1485-1495
    • De Carlo, S.1    Chen, B.2    Hoover, T.R.3    Kondrashkina, E.4    Nogales, E.5    Nixon, B.T.6
  • 35
    • 34250858152 scopus 로고    scopus 로고
    • Functional dynamics of response regulators using NMR relaxation techniques
    • Gardino A.K., and Kern D. Functional dynamics of response regulators using NMR relaxation techniques. Methods Enzymol. 423 (2007) 149-162
    • (2007) Methods Enzymol. , vol.423 , pp. 149-162
    • Gardino, A.K.1    Kern, D.2
  • 36
    • 0033599026 scopus 로고    scopus 로고
    • Structure of a transiently phosphorylated switch in bacterial signal transduction
    • Kern D., Volkman B.F., Luginbuhl P., Nohaile M., Kustu S., and Wemmer D. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature 402 (1999) 898
    • (1999) Nature , vol.402 , pp. 898
    • Kern, D.1    Volkman, B.F.2    Luginbuhl, P.3    Nohaile, M.4    Kustu, S.5    Wemmer, D.6
  • 37
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behaviour in a single-domain signaling protein
    • Volkman B.F., Lipson D., Wemmer D., and Kern D. Two-state allosteric behaviour in a single-domain signaling protein. Science 291 (2001) 2429-2433
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.3    Kern, D.4
  • 38
    • 0026532670 scopus 로고
    • The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription
    • Huala E., Stigter J., and Ausubel F.M. The central domain of Rhizobium leguminosarum DctD functions independently to activate transcription. Bacteriology 174 (1992) 1428-1431
    • (1992) Bacteriology , vol.174 , pp. 1428-1431
    • Huala, E.1    Stigter, J.2    Ausubel, F.M.3
  • 39
    • 0028286432 scopus 로고
    • 54 dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module
    • 54 dependent transcriptional activator, may be negatively controlled by a subdomain in the C-terminal end of its two-component receiver module. Mol. Microbiol. 13 (1994) 51-66
    • (1994) Mol. Microbiol. , vol.13 , pp. 51-66
    • Gu, B.1    Lee, J.2    Hoover, T.R.3    Scholl, D.4    Nixon, B.T.5
  • 40
    • 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. Biochemical evidence for multiple dimeric states of the Sinorhizobium meliloti DctD receiver domain. Biochemistry 41 (2002) 10934-10941
    • (2002) Biochemistry , vol.41 , pp. 10934-10941
    • Park, S.1    Zhang, H.2    Jones, A.D.3    Nixon, B.T.4
  • 43
    • 41149103311 scopus 로고    scopus 로고
    • Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation
    • Wisedchaisri G., Wu M., Sherman D.R., and Hol W.G. Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation. J. Mol. Biol. 378 (2008) 227-242
    • (2008) J. Mol. Biol. , vol.378 , pp. 227-242
    • Wisedchaisri, G.1    Wu, M.2    Sherman, D.R.3    Hol, W.G.4
  • 44
    • 0033566242 scopus 로고    scopus 로고
    • Millisecond-timescale motions contribute to the function of the bacterial response regulator protein SpoOF
    • Feher V.A., and Cavanagh J. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein SpoOF. Lett. Nat. 400 (1999) 289-293
    • (1999) Lett. Nat. , vol.400 , pp. 289-293
    • Feher, V.A.1    Cavanagh, J.2
  • 45
    • 0030850026 scopus 로고    scopus 로고
    • High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator SpoOF: implications for phosphorylation and molecular recognition
    • Feher V.A., Zapf J.W., Hoch J.A., Whiteley J.M., McIntoch L.P., Rance M., et al. High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator SpoOF: implications for phosphorylation and molecular recognition. Biochemistry 36 (1997) 10015-10025
    • (1997) Biochemistry , vol.36 , pp. 10015-10025
    • Feher, V.A.1    Zapf, J.W.2    Hoch, J.A.3    Whiteley, J.M.4    McIntoch, L.P.5    Rance, M.6
  • 47
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 48
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P. Scaling and assessment of data quality. Acta Crystallogr. Sect. D 62 (2006) 72-82
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 49
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A.G. The integration of macromolecular diffraction data. Acta Crystallogr. Sect. D 62 (2006) 48-57
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 50
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates T.O. Detecting and overcoming crystal twinning. Methods Enzymol. 276 (1997) 344-358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 51
    • 0013054388 scopus 로고    scopus 로고
    • Macromolecular phasing with SHELXE
    • Sheldrick G.M. Macromolecular phasing with SHELXE. Z. Kristallogr. 217 (2002) 644-650
    • (2002) Z. Kristallogr. , vol.217 , pp. 644-650
    • Sheldrick, G.M.1
  • 52
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G., Vonrhein C., Flensburg C., Schiltz M., and Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. Sect. D 59 (2003) 2023-2030
    • (2003) Acta Crystallogr. Sect. D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 54
    • 84889120137 scopus 로고
    • Improved methods for building 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47 Pt 2 (1991) 110-119
    • (1991) Acta Crystallogr. Sect. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 56
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. Sect. D 62 (2006) 439-450
    • (2006) Acta Crystallogr. Sect. D , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2


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