메뉴 건너뛰기




Volumn 359, Issue 3, 2006, Pages 798-804

Crystal Structure of Yeast Mitochondrial Peripheral Membrane Protein Tim44p C-terminal Domain

Author keywords

crystal structure; membrane protein; mitochondrion; Tim44

Indexed keywords

MITOCHONDRIAL PROTEIN; MONOMER; PROTEIN TIM44P; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 33646868373     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.04.020     Document Type: Article
Times cited : (30)

References (21)
  • 2
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray M.W., Burger G., and Lang B.F. Mitochondrial evolution. Science 283 (1999) 1476-1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 3
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997) 863-917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 5
    • 0034214123 scopus 로고    scopus 로고
    • Protein sorting: recognizing mitochondrial presequences
    • Pfanner N. Protein sorting: recognizing mitochondrial presequences. Curr. Biol. 10 (2000) R412-R415
    • (2000) Curr. Biol. , vol.10
    • Pfanner, N.1
  • 6
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • Koehler C.M. New developments in mitochondrial assembly. Annu. Rev. Cell Dev. Biol. 20 (2004) 309-335
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 7
    • 0035190910 scopus 로고    scopus 로고
    • A presequence- and voltage-sensitive channel of the mitochondrial preprotein translocase formed by Tim23
    • Truscott K.N., Kovermann P., Geissler A., Merlin A., Meijer M., Driessen A.J., et al. A presequence- and voltage-sensitive channel of the mitochondrial preprotein translocase formed by Tim23. Nature Struct. Biol. 8 (2001) 1074-1082
    • (2001) Nature Struct. Biol. , vol.8 , pp. 1074-1082
    • Truscott, K.N.1    Kovermann, P.2    Geissler, A.3    Merlin, A.4    Meijer, M.5    Driessen, A.J.6
  • 8
    • 0033864758 scopus 로고    scopus 로고
    • Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role
    • Krimmer T., Rassow J., Kunau W.H., Voos W., and Pfanner N. Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role. Mol. Cell. Biol. 20 (2000) 5879-5887
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5879-5887
    • Krimmer, T.1    Rassow, J.2    Kunau, W.H.3    Voos, W.4    Pfanner, N.5
  • 9
    • 0036510606 scopus 로고    scopus 로고
    • Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44
    • Moro F., Okamoto K., Donzeau M., Neupert W., and Brunner M. Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. J. Biol. Chem. 277 (2002) 6874-6880
    • (2002) J. Biol. Chem. , vol.277 , pp. 6874-6880
    • Moro, F.1    Okamoto, K.2    Donzeau, M.3    Neupert, W.4    Brunner, M.5
  • 10
    • 0037013962 scopus 로고    scopus 로고
    • The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria
    • Strub A., Rottgers K., and Voos W. The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria. EMBO J. 21 (2002) 2626-2635
    • (2002) EMBO J. , vol.21 , pp. 2626-2635
    • Strub, A.1    Rottgers, K.2    Voos, W.3
  • 11
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu Q., D'Silva P., Walter W., Marszalek J., and Craig E.A. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300 (2003) 139-141
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 12
    • 7544224771 scopus 로고    scopus 로고
    • Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane
    • D'Silva P., Liu Q., Walter W., and Craig E.A. Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane. Nature Struct. Mol. Biol. 11 (2004) 1084-1091
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 1084-1091
    • D'Silva, P.1    Liu, Q.2    Walter, W.3    Craig, E.A.4
  • 14
    • 33646485126 scopus 로고    scopus 로고
    • Preliminary X-ray crystallographic studies of yeast peripheral mitochondrial membrane protein Tim44p
    • Josyula R., Jin Z., McCombs D., DeLucas L., and Sha B.D. Preliminary X-ray crystallographic studies of yeast peripheral mitochondrial membrane protein Tim44p. Acta Crystallogr. Sect. F 62 (2006) 172-174
    • (2006) Acta Crystallogr. Sect. F , vol.62 , pp. 172-174
    • Josyula, R.1    Jin, Z.2    McCombs, D.3    DeLucas, L.4    Sha, B.D.5
  • 16
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. Sect. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 17
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 20
    • 0000449348 scopus 로고
    • Ribbons 2.0. Ribbon models for macromolecules
    • Carson M. Ribbons 2.0. Ribbon models for macromolecules. J. Mol. Graph. 5 (1987) 103-106
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 21
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.