메뉴 건너뛰기




Volumn 274, Issue 5, 1997, Pages 687-692

Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid

Author keywords

Electron microscopy; HupR; Nickel lipid monolayer; Response regulator; Two dimensional crystallization

Indexed keywords

BACTERIAL PROTEIN; CHELATING AGENT; DIMER; HYDROGENASE; MONOMER; REGULATOR PROTEIN; RESPONSE REGULATOR PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0342722461     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1431     Document Type: Article
Times cited : (46)

References (40)
  • 1
    • 0001328581 scopus 로고
    • Synthesis of new glycerolipids linked to hydroxamate derivatives designed for two-dimensional crystallization of aminopeptidase M
    • Altenburger J. M., Lebeau L., Mioskowski C. Synthesis of new glycerolipids linked to hydroxamate derivatives designed for two-dimensional crystallization of aminopeptidase M. Helv. Chim. Acta. 75:1992;2538-2544.
    • (1992) Helv. Chim. Acta , vol.75 , pp. 2538-2544
    • Altenburger, J.M.1    Lebeau, L.2    Mioskowski, C.3
  • 2
    • 0029670614 scopus 로고    scopus 로고
    • Visualisation of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography
    • Avila-Sakar A. J., Chiu W. Visualisation of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys. J. 70:1996;57-68.
    • (1996) Biophys. J. , vol.70 , pp. 57-68
    • Avila-Sakar, A.J.1    Chiu, W.2
  • 5
    • 0028244638 scopus 로고
    • Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface
    • Bellsolell L., Prieto J., Serrano L., Coll M. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J. Mol. Biol. 238:1994;489-495.
    • (1994) J. Mol. Biol. , vol.238 , pp. 489-495
    • Bellsolell, L.1    Prieto, J.2    Serrano, L.3    Coll, M.4
  • 7
    • 0024284362 scopus 로고
    • The effect on the function of the transcriptional activator NtrC fromKlebsiella pneumoniae
    • Contreras A., Drummond M. The effect on the function of the transcriptional activator NtrC fromKlebsiella pneumoniae. Nucleic Acids Res. 16:1988;4025-4039.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 4025-4039
    • Contreras, A.1    Drummond, M.2
  • 9
    • 0014817347 scopus 로고
    • Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins
    • Davies G. E., Stark G. R. Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc. Natl Acad. Sci. USA. 66:1970;651-656.
    • (1970) Proc. Natl Acad. Sci. USA , vol.66 , pp. 651-656
    • Davies, G.E.1    Stark, G.R.2
  • 10
    • 0029025914 scopus 로고
    • Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipid
    • Dietrich C., Schmitt L., Tampé R. Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipid. Proc. Natl Acad. Sci. USA. 92:1995;9014-9018.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9014-9018
    • Dietrich, C.1    Schmitt, L.2    Tampé, R.3
  • 11
    • 0030069974 scopus 로고    scopus 로고
    • Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids
    • Dietrich C., Boscheinen O., Scharf K.-D., Schmitt L., Tampé R. Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids. Biochemistry. 35:1996;1100-1105.
    • (1996) Biochemistry , vol.35 , pp. 1100-1105
    • Dietrich, C.1    Boscheinen, O.2    Scharf, K.-D.3    Schmitt, L.4    Tampé, R.5
  • 12
    • 0022668501 scopus 로고
    • Sequence and domain relationships of NtrC and nifA fromKlebsiella pneumoniae
    • Drummond M., Whitty P., Wootton J. Sequence and domain relationships of NtrC and nifA fromKlebsiella pneumoniae. EMBO J. 5:1986;441-447.
    • (1986) EMBO J. , vol.5 , pp. 441-447
    • Drummond, M.1    Whitty, P.2    Wootton, J.3
  • 13
    • 0029164694 scopus 로고
    • A common switch in activation of the response regulators NtrC and PhoB: Phosphorylation induces dimerization of the receiver modules
    • Fiedler U., Weiss V. A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules. EMBO J. 14:1995;3696-3705.
    • (1995) EMBO J. , vol.14 , pp. 3696-3705
    • Fiedler, U.1    Weiss, V.2
  • 14
  • 15
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J., Ceska T., Zemlin F., Beckmann E., Downing K. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.2    Ceska, T.3    Zemlin, F.4    Beckmann, E.5    Downing, K.6
  • 17
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Döbeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatog. 411:1987;177-184.
    • (1987) J. Chromatog. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 18
    • 0027176130 scopus 로고
    • Purification and characterization of a novel dimeric ferredoxin (FdIII) fromRhodobacter capsulatus
    • Jouanneau Y., Meyer C., Gaillard J., Forest E., Gagnon J. Purification and characterization of a novel dimeric ferredoxin (FdIII) fromRhodobacter capsulatus. J. Biol. Chem. 268:1993;10636-10644.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10636-10644
    • Jouanneau, Y.1    Meyer, C.2    Gaillard, J.3    Forest, E.4    Gagnon, J.5
  • 19
    • 0024040412 scopus 로고
    • Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: Roles of the conserved amino-terminal domain of NTRC
    • Keener J., Kustu S. Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC. Proc. Natl Acad. Sci. USA. 85:1988;4976-4980.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4976-4980
    • Keener, J.1    Kustu, S.2
  • 20
    • 0028122355 scopus 로고
    • The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain
    • Klose K. E., North A. K., Stedman K. M., Kustu S. The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain. J. Mol. Biol. 241:1994;233-245.
    • (1994) J. Mol. Biol. , vol.241 , pp. 233-245
    • Klose, K.E.1    North, A.K.2    Stedman, K.M.3    Kustu, S.4
  • 21
    • 0028590161 scopus 로고
    • Two-dimensional crystallization of histidine-tagged HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid
    • Kubalek E., Le Grice S., Brown P. Two-dimensional crystallization of histidine-tagged HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 113:1994;117-123.
    • (1994) J. Struct. Biol. , vol.113 , pp. 117-123
    • Kubalek, E.1    Le Grice, S.2    Brown, P.3
  • 22
    • 0028147508 scopus 로고
    • Atomic model of plant-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D. N., Fujiyhoshi Y. Atomic model of plant-harvesting complex by electron crystallography. Nature. 367:1994;614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyhoshi, Y.3
  • 23
    • 0025938894 scopus 로고
    • Prokaryotic transcriptional enhancers and enhancer-binding proteins
    • Kustu S., North A. K., Weiss D. S. Prokaryotic transcriptional enhancers and enhancer-binding proteins. Trends Biochem. Sci. 16:1991;397-402.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 397-402
    • Kustu, S.1    North, A.K.2    Weiss, D.S.3
  • 24
    • 0029148094 scopus 로고
    • Mechanism of activation of a response regulator: Interaction of NtrC-P dimers induces ATPase activity
    • Mettke I., Fiedler U., Weiss V. Mechanism of activation of a response regulator: Interaction of NtrC-P dimers induces ATPase activity. J. Bacteriol. 177:1995;5056-5061.
    • (1995) J. Bacteriol. , vol.177 , pp. 5056-5061
    • Mettke, I.1    Fiedler, U.2    Weiss, V.3
  • 25
    • 27644486706 scopus 로고
    • Engineering protein-lipid interactions: Targeting of histidine-tagged proteins to metal-chelating lipid monolayers
    • Ng K., Pack D., Sasaki D., Arnold F. Engineering protein-lipid interactions: targeting of histidine-tagged proteins to metal-chelating lipid monolayers. Langmuir. 11:1995;4048-4055.
    • (1995) Langmuir , vol.11 , pp. 4048-4055
    • Ng, K.1    Pack, D.2    Sasaki, D.3    Arnold, F.4
  • 26
    • 0028631772 scopus 로고
    • Two-dimensional structure of membrane-bound annexin V at 8 Å resolution
    • Olofsson A., Mallouh V., Brisson A. Two-dimensional structure of membrane-bound annexin V at 8 Å resolution. J. Struct. Biol. 113:1994;199-205.
    • (1994) J. Struct. Biol. , vol.113 , pp. 199-205
    • Olofsson, A.1    Mallouh, V.2    Brisson, A.3
  • 27
    • 0030901962 scopus 로고    scopus 로고
    • A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines
    • Pack D. W., Chen G., Maloney K. M., Chen C.-T., Arnold F. H. A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines. J. Am. Chem. Soc. 119:1997;2479-2487.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2479-2487
    • Pack, D.W.1    Chen, G.2    Maloney, K.M.3    Chen, C.-T.4    Arnold, F.H.5
  • 28
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson J. S., Kofoid E. C. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:1992;71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 31
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W. O., Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127:1982;127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 32
  • 33
    • 0024066462 scopus 로고
    • Introduction to the computer image processing of electron micrographs of two-dimensionally ordered biological structures
    • Stewart M. Introduction to the computer image processing of electron micrographs of two-dimensionally ordered biological structures. J. Electron Microsc. Tech. 9:1988;301-324.
    • (1988) J. Electron Microsc. Tech. , vol.9 , pp. 301-324
    • Stewart, M.1
  • 34
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock A. M., Mottonen J. M., Stock B., Schutt C. E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature. 337:1989;745-749.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, B.3    Schutt, C.E.4
  • 36
    • 0020691229 scopus 로고
    • Two-dimensional crystallization technique for imaging macromolecules with application to antigen-antibody-complement complexes
    • Uzgiris E., Kornberg R. Two-dimensional crystallization technique for imaging macromolecules with application to antigen-antibody-complement complexes. Nature. 301:1983;125-129.
    • (1983) Nature , vol.301 , pp. 125-129
    • Uzgiris, E.1    Kornberg, R.2
  • 37
    • 0028795614 scopus 로고
    • Effect of C-terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes
    • Venien-Bryan C., Davies A., Langmark K., Baverstock J., Watts A., Marsh D., Saibil H. Effect of C-terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes. FEBS Letters. 359:1995;45-49.
    • (1995) FEBS Letters , vol.359 , pp. 45-49
    • Venien-Bryan, C.1    Davies, A.2    Langmark, K.3    Baverstock, J.4    Watts, A.5    Marsh, D.6    Saibil, H.7
  • 38
    • 0002226012 scopus 로고
    • Regulation of hydrogenase gene expression
    • Dordrecht, Boston, London: Kluwer Academic Publisher
    • Vignais P. M., Toussaint B., Colbeau A. Regulation of hydrogenase gene expression. Anoxygenic Photosynthetic Bacteria. 1995;Kluwer Academic Publisher, Dordrecht, Boston, London.
    • (1995) Anoxygenic Photosynthetic Bacteria
    • Vignais, P.M.1    Toussaint, B.2    Colbeau, A.3
  • 39
    • 0028927334 scopus 로고
    • Three-dimensional solution structure of the N-terminal receiver domain of NTRC
    • Volkman B. F., Nohaile M. J., Amy N. K., Kustu S., Wemmer D. E. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 34:1995;1413-1424.
    • (1995) Biochemistry , vol.34 , pp. 1413-1424
    • Volkman, B.F.1    Nohaile, M.J.2    Amy, N.K.3    Kustu, S.4    Wemmer, D.E.5
  • 40
    • 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., 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.