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Volumn 144, Issue 3, 2003, Pages 313-319

Crystal structure of SecB from Escherichia coli

Author keywords

Chaperone; Crystal structure; Escherichia coli; Protein translocation; SecB

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; PROTEIN PRECURSOR; PROTEIN SECA; PROTEIN SECB; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0344983315     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.09.012     Document Type: Article
Times cited : (55)

References (31)
  • 3
    • 0028103275 scopus 로고
    • Collaborative Computational Project No. 4: The CCP4 suite: Programs for protein crystallography
    • CCP4. 1994. Collaborative Computational Project No. 4: The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 6
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • Driessen A.J.M., Manting E.H., van der Does C. The structural basis of protein targeting and translocation in bacteria. Nat. Struct. Biol. 8:2001;492-498.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 492-498
    • Driessen, A.J.M.1    Manting, E.H.2    Van Der Does, C.3
  • 7
    • 0031656854 scopus 로고    scopus 로고
    • Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA
    • Fekkes P., de Wit J.G., van der Wolk J.P.W., Kimsey H.H., Kumamoto C.A., Driessen A.J.M. Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol. Microbiol. 29:1998;1179-1190.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1179-1190
    • Fekkes, P.1    De Wit, J.G.2    Van Der Wolk, J.P.W.3    Kimsey, H.H.4    Kumamoto, C.A.5    Driessen, A.J.M.6
  • 8
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • Fekkes P., van der Does C., Driessen A.J.M. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. EMBO J. 16:1997;6105-6113.
    • (1997) EMBO J. , vol.16 , pp. 6105-6113
    • Fekkes, P.1    Van Der Does, C.2    Driessen, A.J.M.3
  • 9
    • 0025036708 scopus 로고
    • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
    • Hartl F.-U., Lecker S., Schiebel E., Hendrick J.P., Wickner W. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell. 63:1990;269-279.
    • (1990) Cell , vol.63 , pp. 269-279
    • Hartl, F.-U.1    Lecker, S.2    Schiebel, E.3    Hendrick, J.P.4    Wickner, W.5
  • 10
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science. 297:2002;2018-2026.
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 11
    • 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 J.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, J.W.3    Kjeldgaard, M.4
  • 12
    • 0028875765 scopus 로고
    • Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein
    • Khisty V.J., Munske G.R., Randall L.L. Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein. J. Biol. Chem. 270:1995;25920-25927.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25920-25927
    • Khisty, V.J.1    Munske, G.R.2    Randall, L.L.3
  • 13
    • 0029128122 scopus 로고
    • Diverse effect of mutation on the activity of the Escherichia coli export chaperone SecB
    • Kimsey H.H., Dagarag M.D., Kumamoto C.A. Diverse effect of mutation on the activity of the Escherichia coli export chaperone SecB. J. Biol. Chem. 270:1995;22831-22835.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22831-22835
    • Kimsey, H.H.1    Dagarag, M.D.2    Kumamoto, C.A.3
  • 15
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 16
    • 0025296933 scopus 로고
    • SecB protein: A cytosolic export factor that associates with nascent exported proteins
    • Kumamoto C. SecB protein: a cytosolic export factor that associates with nascent exported proteins. J. Bioenerg. Biomem. 22:1990;337-351.
    • (1990) J. Bioenerg. Biomem. , vol.22 , pp. 337-351
    • Kumamoto, C.1
  • 17
    • 0033516465 scopus 로고    scopus 로고
    • Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers
    • Muren E.M., Suciu D., Topping T.B., Kumamoto C.A., Randall L.L. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers. J. Biol. Chem. 274:1999;19397-19402.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19397-19402
    • Muren, E.M.1    Suciu, D.2    Topping, T.B.3    Kumamoto, C.A.4    Randall, L.L.5
  • 18
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 19
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 20
    • 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
  • 21
    • 0034705529 scopus 로고    scopus 로고
    • A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone SecB
    • Panse V.G., Vogel P., Trommer W.E., Varadarajan R. A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone SecB. J. Biol. Chem. 275:2000;18698-18703.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18698-18703
    • Panse, V.G.1    Vogel, P.2    Trommer, W.E.3    Varadarajan, R.4
  • 22
    • 0026755898 scopus 로고
    • Peptide binding by chaperone SecB: Implications for recognition of nonnative structure
    • Randall L.L. Peptide binding by chaperone SecB: implications for recognition of nonnative structure. Science. 257:1992;241-245.
    • (1992) Science , vol.257 , pp. 241-245
    • Randall, L.L.1
  • 23
    • 0031734169 scopus 로고    scopus 로고
    • The interaction between the chaperone SecB and its ligands: Evidence for multiple subsites for binding
    • Randall L.L., Hardy S., Topping T.B., Smith V.F., Bruce J.E., Smith R.D. The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding. Protein Sci. 7:1998;2384-2390.
    • (1998) Protein Sci. , vol.7 , pp. 2384-2390
    • Randall, L.L.1    Hardy, S.2    Topping, T.B.3    Smith, V.F.4    Bruce, J.E.5    Smith, R.D.6
  • 24
    • 0033669539 scopus 로고    scopus 로고
    • The promiscuous and specific sides of SecB
    • Randall L.L., Hardy S.J. The promiscuous and specific sides of SecB. Nat. Struct. Biol. 7:2000;1077-1079.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1077-1079
    • Randall, L.L.1    Hardy, S.J.2
  • 25
    • 0036809395 scopus 로고    scopus 로고
    • SecB, one small chaperone in the complex milieu of the cell
    • Randall L.L., Hardy S.J. SecB, one small chaperone in the complex milieu of the cell. Cell. Mol. Life Sci. 59:2002;1617-1623.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1617-1623
    • Randall, L.L.1    Hardy, S.J.2
  • 26
    • 0028831186 scopus 로고
    • High selectivity with low specificity: How SecB has solved the paradox of chaperone binding
    • Randall L.L., Hardy S.J.S. High selectivity with low specificity: how SecB has solved the paradox of chaperone binding. TIBS. 20:1995;65-69.
    • (1995) TIBS , vol.20 , pp. 65-69
    • Randall, L.L.1    Hardy, S.J.S.2
  • 27
    • 0030798169 scopus 로고    scopus 로고
    • Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands
    • Topping T., Randall L.L. Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. J. Biol. Chem. 272:1997;19314-19318.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19314-19318
    • Topping, T.1    Randall, L.L.2
  • 28
    • 0028214003 scopus 로고
    • Determination of the binding frame within a physiological ligand for the chaperone SecB
    • Topping T.B., Randall L.L. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 3:1994;730-736.
    • (1994) Protein Sci. , vol.3 , pp. 730-736
    • Topping, T.B.1    Randall, L.L.2
  • 29
    • 0035831535 scopus 로고    scopus 로고
    • Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium
    • Topping T.B., Woodbury R.L., Diamond D.L., Hardy S.J., Randall L.L. Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium. J. Biol. Chem. 276:2001;7437-7441.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7437-7441
    • Topping, T.B.1    Woodbury, R.L.2    Diamond, D.L.3    Hardy, S.J.4    Randall, L.L.5
  • 30
    • 0033517829 scopus 로고    scopus 로고
    • A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB
    • Volkert T.L., Baleja J.D., Kumamoto C.A. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. Biochem. Biophys. Res. Commun. 264:1999;949-954.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 949-954
    • Volkert, T.L.1    Baleja, J.D.2    Kumamoto, C.A.3
  • 31
    • 0033675260 scopus 로고    scopus 로고
    • Crystal structure of the bacterial protein export chaperone SecB
    • Xu Z., Knafels J.D., Yoshino K. Crystal structure of the bacterial protein export chaperone SecB. Nat. Struct. Biol. 7:2000;1172-1177.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1172-1177
    • Xu, Z.1    Knafels, J.D.2    Yoshino, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.