메뉴 건너뛰기




Volumn 15, Issue 3, 2004, Pages 367-374

Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; LIPOPOLYSACCHARIDE; MEMBRANE PROTEIN;

EID: 4143114616     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.07.023     Document Type: Article
Times cited : (177)

References (37)
  • 1
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann H., Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat. Biotechnol. 16:1998;376-380
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 3
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 278:2003;9092-9099
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 4
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen R., Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19:1996;1287-1294
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 5
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
    • Danese P.N., Silhavy T.J. Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli. Annu. Rev. Genet. 32:1998;59-94
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 6
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein
    • De Cock H., Schafer U., Potgeter M., Demel R., Muller M., Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259:1999;96-103
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • De Cock, H.1    Schafer, U.2    Potgeter, M.3    Demel, R.4    Muller, M.5    Tommassen, J.6
  • 7
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • Driessen A.J., 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.1    Manting, E.H.2    Van Der Does, C.3
  • 8
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport. crystal structure of FhuA with bound lipopolysaccharide Science. 282:1998;2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 9
    • 0018365893 scopus 로고
    • A lipopolysaccharide-binding cell-surface protein from Salmonella minnesota. Isolation, partial characterization and occurrence in different Enterobacteriaceae
    • Geyer R., Galanos C., Westphal O., Golecki J.R. A lipopolysaccharide- binding cell-surface protein from Salmonella minnesota. Isolation, partial characterization and occurrence in different Enterobacteriaceae. Eur. J. Biochem. 98:1979;27-38
    • (1979) Eur. J. Biochem. , vol.98 , pp. 27-38
    • Geyer, R.1    Galanos, C.2    Westphal, O.3    Golecki, J.R.4
  • 10
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane
    • Harms N., Koningstein G., Dontje W., Muller M., Oudega B., Luirink J., de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 276:2001;18804-18811
    • (2001) J. Biol. Chem. , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4    Oudega, B.5    Luirink, J.6    De Cock, H.7
  • 11
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol. from nascent chain to folded protein Science. 295:2002;1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 12
    • 0033117352 scopus 로고    scopus 로고
    • Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments
    • Hayhurst A., Harris W.J. Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments. Protein Expr. Purif. 15:1999;336-343
    • (1999) Protein Expr. Purif. , vol.15 , pp. 336-343
    • Hayhurst, A.1    Harris, W.J.2
  • 13
    • 0025263809 scopus 로고
    • Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent?
    • Hirvas L., Coleman J., Koski P., Vaara M. Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent? FEBS Lett. 262:1990;123-126
    • (1990) FEBS Lett. , vol.262 , pp. 123-126
    • Hirvas, L.1    Coleman, J.2    Koski, P.3    Vaara, M.4
  • 14
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr. 11:1978;268-272
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, A.1
  • 15
    • 0032832765 scopus 로고    scopus 로고
    • Outer membrane protein a of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
    • Kleinschmidt J.H., Wiener M.C., Tamm L.K. Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent. Protein Sci. 8:1999;2065-2071
    • (1999) Protein Sci. , vol.8 , pp. 2065-2071
    • Kleinschmidt, J.H.1    Wiener, M.C.2    Tamm, L.K.3
  • 16
    • 0025280947 scopus 로고
    • Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium
    • Koski P., Hirvas L., Vaara M. Complete sequence of the ompH gene encoding the 16-kDa cationic outer membrane protein of Salmonella typhimurium. Gene. 88:1990;117-120
    • (1990) Gene , vol.88 , pp. 117-120
    • Koski, P.1    Hirvas, L.2    Vaara, M.3
  • 17
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. 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.1
  • 19
    • 0033943049 scopus 로고    scopus 로고
    • Escherichia coli translocase: The unravelling of a molecular machine
    • Manting E.H., Driessen A.J. Escherichia coli translocase. the unravelling of a molecular machine Mol. Microbiol. 37:2000;226-238
    • (2000) Mol. Microbiol. , vol.37 , pp. 226-238
    • Manting, E.H.1    Driessen, A.J.2
  • 21
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 22
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D., Raina S. Protein folding in the bacterial periplasm. J. Bacteriol. 179:1997;2465-2471
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 23
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D., Betton J.M., Raina S. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21:1996;871-884
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 24
    • 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. 11:1991;281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 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
  • 26
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen M.J., Wren B.W. The HtrA family of serine proteases. Mol. Microbiol. 26:1997;209-221
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 27
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schafer U., Beck K., Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274:1999;24567-24574
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schafer, U.1    Beck, K.2    Muller, M.3
  • 28
    • 1842787813 scopus 로고    scopus 로고
    • The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization
    • Schlapschy M., Dommel M.K., Hadian K., Fogarasi M., Korndorfer I.P., Skerra A. The periplasmic E. coli chaperone Skp is a trimer in solution. biophysical and preliminary crystallographic characterization Biol. Chem. 385:2004;137-143
    • (2004) Biol. Chem. , vol.385 , pp. 137-143
    • Schlapschy, M.1    Dommel, M.K.2    Hadian, K.3    Fogarasi, M.4    Korndorfer, I.P.5    Skerra, A.6
  • 29
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert R., Leroux M.R., Scheufler C., Hartl F.U., Moarefi I. Structure of the molecular chaperone prefoldin. unique interaction of multiple coiled coil tentacles with unfolded proteins Cell. 103:2000;621-632
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 31
    • 0030045746 scopus 로고    scopus 로고
    • Folding and membrane insertion of the trimeric beta-barrel protein OmpF
    • Surrey T., Schmid A., Jahnig F. Folding and membrane insertion of the trimeric beta-barrel protein OmpF. Biochemistry. 35:1996;2283-2288
    • (1996) Biochemistry , vol.35 , pp. 2283-2288
    • Surrey, T.1    Schmid, A.2    Jahnig, F.3
  • 32
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • a
    • Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallogr. D. 58:2002;1937-1940. a
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 33
    • 0036900870 scopus 로고    scopus 로고
    • Rapid automatic NCS identification using heavy-atom substructures
    • b
    • Terwilliger T.C. Rapid automatic NCS identification using heavy-atom substructures. Acta Crystallogr. D. 58:2002;2213-2215. b
    • (2002) Acta Crystallogr. D , vol.58 , pp. 2213-2215
    • Terwilliger, T.C.1
  • 34
    • 0036901176 scopus 로고    scopus 로고
    • Statistical density modification with non-crystallographic symmetry
    • c
    • Terwilliger T.C. Statistical density modification with non-crystallographic symmetry. Acta Crystallogr. D. 58:2002;2082-2086. c
    • (2002) Acta Crystallogr. D , vol.58 , pp. 2082-2086
    • Terwilliger, T.C.1
  • 35
    • 2142689200 scopus 로고    scopus 로고
    • Solve and resolve: Automated structure solution, density modification and model building
    • Terwilliger T. Solve and resolve. automated structure solution, density modification and model building J. Synchrotron Radiat. 11:2004;49-52
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 37
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 388:1997;741-750
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.