메뉴 건너뛰기




Volumn 1702, Issue 2, 2004, Pages 163-171

NMR structure of the C-terminal domain of SecA in the free state

Author keywords

NMR structure; Protein interaction; SecA; SecB; Secretory translocase; Zinc finger

Indexed keywords

CHAPERONE; ZINC;

EID: 5444276532     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.08.012     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0032747644 scopus 로고    scopus 로고
    • SecA: The ubiquitous component of preprotein translocase in prokaryotes
    • M.G. Schmidt, and K.B. Kiser SecA: the ubiquitous component of preprotein translocase in prokaryotes Microbes Infect. 1 1999 993 1004
    • (1999) Microbes Infect. , vol.1 , pp. 993-1004
    • Schmidt, M.G.1    Kiser, K.B.2
  • 3
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • A.J. Driessen, E.H. Manting, and C. van der Does 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
  • 4
    • 0035477117 scopus 로고    scopus 로고
    • The Sec protein-translocation pathway
    • H. Mori, and K. Ito The Sec protein-translocation pathway Trends Microbiol. 9 2001 494 500
    • (2001) Trends Microbiol. , vol.9 , pp. 494-500
    • Mori, H.1    Ito, K.2
  • 5
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • J.F. Hunt, S. Weinkauf, L. Henry, J.J. Fak, P. McNicholas, D.B. Oliver, and J. Deisenhofer 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
  • 8
    • 0242407175 scopus 로고    scopus 로고
    • Structural determinants of SecB recognition by SecA in bacterial protein translocation
    • J. Zhou, and Z. Xu Structural determinants of SecB recognition by SecA in bacterial protein translocation Nat. Struct. Biol. 10 2003 942 947
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 942-947
    • Zhou, J.1    Xu, Z.2
  • 9
    • 1842559293 scopus 로고    scopus 로고
    • Sites of interaction between SecA and the chaperone SecB, two proteins involved in export
    • L.L. Randall, J.M. Crane, G. Liu, and S.J. Hardy Sites of interaction between SecA and the chaperone SecB, two proteins involved in export Protein Sci. 13 2004 1124 1133
    • (2004) Protein Sci. , vol.13 , pp. 1124-1133
    • Randall, L.L.1    Crane, J.M.2    Liu, G.3    Hardy, S.J.4
  • 10
    • 0036931270 scopus 로고    scopus 로고
    • Zinc fingers-folds for many occasions
    • J.M. Matthews, and M. Sunde Zinc fingers-folds for many occasions IUBMB Life 54 2002 351 355
    • (2002) IUBMB Life , vol.54 , pp. 351-355
    • Matthews, J.M.1    Sunde, M.2
  • 12
    • 0033609448 scopus 로고    scopus 로고
    • Structural investigation on the requirement of CCHH zinc finger type in nucleocapsid protein of human immunodeficiency virus 1
    • S. Ramboarina, N. Morellet, M.C. Fournie-Zaluski, B.P. Roques, and N. Moreller Structural investigation on the requirement of CCHH zinc finger type in nucleocapsid protein of human immunodeficiency virus 1 Biochemistry 38 1999 9600 9607
    • (1999) Biochemistry , vol.38 , pp. 9600-9607
    • Ramboarina, S.1    Morellet, N.2    Fournie-Zaluski, M.C.3    Roques, B.P.4    Moreller, N.5
  • 13
    • 0034692876 scopus 로고    scopus 로고
    • Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP
    • R.N. De Guzman, H.Y. Liu, M. Martinez-Yamout, H.J. Dyson, and P.E. Wright Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP J. Mol. Biol. 303 2000 243 253
    • (2000) J. Mol. Biol. , vol.303 , pp. 243-253
    • De Guzman, R.N.1    Liu, H.Y.2    Martinez-Yamout, M.3    Dyson, H.J.4    Wright, P.E.5
  • 14
    • 0346036165 scopus 로고    scopus 로고
    • Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR
    • Y.T. Chou, J.F. Swain, and L.M. Gierasch Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR J. Biol. Chem. 277 2002 50985 50990
    • (2002) J. Biol. Chem. , vol.277 , pp. 50985-50990
    • Chou, Y.T.1    Swain, J.F.2    Gierasch, L.M.3
  • 16
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 17
    • 0042346328 scopus 로고    scopus 로고
    • CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions
    • R.J. Simpson, E.D. Cram, R. Czolij, J.M. Matthews, M. Crossley, and J.P. Mackay CCHX zinc finger derivatives retain the ability to bind Zn(II) and mediate protein-DNA interactions J. Biol. Chem. 278 2003 28011 28018
    • (2003) J. Biol. Chem. , vol.278 , pp. 28011-28018
    • Simpson, R.J.1    Cram, E.D.2    Czolij, R.3    Matthews, J.M.4    Crossley, M.5    MacKay, J.P.6
  • 20
    • 0028672867 scopus 로고
    • Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins
    • D.A. Case, H.J. Dyson, and P.E. Wright Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins Methods Enzymol. 239 1994 392 416
    • (1994) Methods Enzymol. , vol.239 , pp. 392-416
    • Case, D.A.1    Dyson, H.J.2    Wright, P.E.3
  • 21
    • 0037877123 scopus 로고
    • A system for X-ray crystallography and NMR
    • Yale University Press New Haven
    • A.T. Brunger A system for X-ray crystallography and NMR X-PLOR Version 3.1 1992 Yale University Press New Haven
    • (1992) X-PLOR Version 3.1
    • Brunger, A.T.1
  • 22
    • 0021095743 scopus 로고
    • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance
    • K. Wuthrich, M. Billeter, and W. Braun Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance J. Mol. Biol. 169 1983 949 961
    • (1983) J. Mol. Biol. , vol.169 , pp. 949-961
    • Wuthrich, K.1    Billeter, M.2    Braun, W.3
  • 24
    • 17044446282 scopus 로고    scopus 로고
    • NMR studies of structure and function of biological macromolecules (Nobel lecture)
    • K. Wuthrich NMR studies of structure and function of biological macromolecules (Nobel lecture) Angew. Chem., Int. Ed. Engl. 42 2003 3340 3363
    • (2003) Angew. Chem., Int. Ed. Engl. , vol.42 , pp. 3340-3363
    • Wuthrich, K.1
  • 25
    • 0025366064 scopus 로고
    • Coupling between local structure and global stability of a protein: Mutants of staphylococcal nuclease
    • A.T. Alexandrescu, A.P. Hinck, and J.L. Markley Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease Biochemistry 29 1990 4516 4525
    • (1990) Biochemistry , vol.29 , pp. 4516-4525
    • Alexandrescu, A.T.1    Hinck, A.P.2    Markley, J.L.3
  • 27
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • E.G. Hutchinson, and J.M. Thornton A revised set of potentials for beta-turn formation in proteins Protein Sci. 3 1994 2207 2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 28
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • L. Holm, and C. Sander Dali: a network tool for protein structure comparison Trends Biochem. Sci. 20 1995 478 480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 29
    • 0030703175 scopus 로고    scopus 로고
    • The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
    • P. Fekkes, C. van der Does, and A.J. Driessen 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.3
  • 30
    • 0242320522 scopus 로고    scopus 로고
    • The bacterial translocase: A dynamic protein channel complex
    • J. de Keyzer, C. van der Does, and A.J. Driessen The bacterial translocase: a dynamic protein channel complex Cell. Mol. Life Sci. 60 2003 2034 2052
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2034-2052
    • De Keyzer, J.1    Van Der Does, C.2    Driessen, A.J.3
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT-a program to produce both detailed and schematic plots of protein structure
    • P.J. Kraulis MOLSCRIPT-a program to produce both detailed and schematic plots of protein structure J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • N.P. Pavletich, and C.O. Pabo Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å Science 252 1991 809 817
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.