메뉴 건너뛰기




Volumn 58, Issue 2, 2005, Pages 498-500

Crystal structure of the co-chaperonin Cpn10 from Thermus thermophilus HB8

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; MONOMER; PROTEIN SUBUNIT;

EID: 11344283815     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20317     Document Type: Article
Times cited : (11)

References (21)
  • 1
    • 0344738987 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: Fate of substrate polypeptide
    • Fenton WA, Horwich AL. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q Rev Biophys 2003;36:229-256.
    • (2003) Q Rev Biophys , vol.36 , pp. 229-256
    • Fenton, W.A.1    Horwich, A.L.2
  • 2
    • 0036809967 scopus 로고    scopus 로고
    • Structure and function of the GroE chaperone
    • Walter S. Structure and function of the GroE chaperone. Cell Mol Life Sci 2002;59:1589-1597.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1589-1597
    • Walter, S.1
  • 3
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 1999;97:325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 4
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z, Horwich AL, Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997;388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 6
    • 0036008510 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution
    • Taneja B, Mande SC. Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 A resolution. Acta Crystallogr D Biol Crystallogr 2002;58:260-266.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 260-266
    • Taneja, B.1    Mande, S.C.2
  • 7
    • 0037924463 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops
    • Roberts MM, Coker AR, Fossati G, Mascagni P, Coates AR, Wood SP. Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops. J Bacteriol 2003;185:4172-4185.
    • (2003) J Bacteriol , vol.185 , pp. 4172-4185
    • Roberts, M.M.1    Coker, A.R.2    Fossati, G.3    Mascagni, P.4    Coates, A.R.5    Wood, S.P.6
  • 8
    • 0030031059 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    • Mande SC, Mehra V, Bloom BR, Hol WG. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Science 1996;271:203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.4
  • 9
    • 0030792944 scopus 로고    scopus 로고
    • Structural adaptations in the specialized bacteriophage T4 co-chaperonin GpS1 expand the size of the Anfinsen cage
    • Hunt JF, van der Vies SM, Henry L, Deisenhofer J. Structural adaptations in the specialized bacteriophage T4 co-chaperonin GpS1 expand the size of the Anfinsen cage. Cell 1997;90:361-371.
    • (1997) Cell , vol.90 , pp. 361-371
    • Hunt, J.F.1    Van Der Vies, S.M.2    Henry, L.3    Deisenhofer, J.4
  • 11
    • 0029745707 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis heat shock protein 10 increases both proliferation and death in mouse P19 teratocarcinoma cells
    • Galli G, Ghezzi P, Mascagni P, Marcucci F, Fratelli M. Mycobacterium tuberculosis heat shock protein 10 increases both proliferation and death in mouse P19 teratocarcinoma cells. In Vitro Cell Dev Biol Anim 1996;32:446-450.
    • (1996) In Vitro Cell Dev Biol Anim , vol.32 , pp. 446-450
    • Galli, G.1    Ghezzi, P.2    Mascagni, P.3    Marcucci, F.4    Fratelli, M.5
  • 12
    • 0027466891 scopus 로고
    • Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate
    • Taguchi H, Yoshida M. Chaperonin from Thermus thermophilus can protect several enzymes from irreversible heat denaturation by capturing denaturation intermediate. J Biol Chem 1993;268:5371-5375.
    • (1993) J Biol Chem , vol.268 , pp. 5371-5375
    • Taguchi, H.1    Yoshida, M.2
  • 13
    • 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 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr A 1994;50:157-163.
    • (1994) Acta Crystallogr A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 17
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS, Thornton JM. Main-chain bond lengths and bond angles in protein structures. J Mol Biol 1993;231:1049-1067.
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 18
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No.4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 19
    • 0141527459 scopus 로고    scopus 로고
    • Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering
    • Higurashi T, Hiragi Y, Ichimura K, Seki Y, Soda K, Mizobata T, Kawata Y. Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering. J Mol Biol 2003;333:605-620.
    • (2003) J Mol Biol , vol.333 , pp. 605-620
    • Higurashi, T.1    Hiragi, Y.2    Ichimura, K.3    Seki, Y.4    Soda, K.5    Mizobata, T.6    Kawata, Y.7
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures
    • Kraulis PJ. MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit EA, Bacon DJ. Raster3D: photorealistic molecular graphics. Meth Enzymol 1997;277:505-524.
    • (1997) Meth Enzymol , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.