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Volumn 114, Issue 2-3, 2005, Pages 181-189

Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold

Author keywords

CheY; Cutinase; Flavodoxin; Folding intermediate; Protein folding; Topology

Indexed keywords

APOFLAVODOXIN; BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIAL TOXIN; CUTINASE; FLAVODOXIN; PROTEIN; PROTEIN CHEY; UNCLASSIFIED DRUG;

EID: 17144415198     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.12.005     Document Type: Article
Times cited : (42)

References (30)
  • 1
    • 0032707954 scopus 로고    scopus 로고
    • Finding the right fold
    • D.P. Goldberg Finding the right fold Nat. Struct. Biol. 6 1999 987 990
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 987-990
    • Goldberg, D.P.1
  • 2
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • D. Baker A surprising simplicity to protein folding Nature 405 2000 39 42
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 3
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures
    • E. Alm, and D. Baker Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures Proc. Natl. Acad. Sci. U. S. A. 96 1999 11305 11310
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 5
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • A.R. Fersht, A. Matouschek, and L. Serrano The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding J. Mol. Biol. 224 1992 771 782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 7
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • J.C. Martinez, and L. Serrano The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved Nat. Struct. Biol. 6 1999 1010 1016
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 8
    • 2342451295 scopus 로고    scopus 로고
    • Transition states for protein folding have native topologies despite high structural variability
    • K. Lindorff-Larsen, M. Vendruscolo, E. Paci, and C.M. Dobson Transition states for protein folding have native topologies despite high structural variability Nat. Struct. Mol. Biol. 11 2004 443 449
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 443-449
    • Lindorff-Larsen, K.1    Vendruscolo, M.2    Paci, E.3    Dobson, C.M.4
  • 9
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain
    • V. Villegas, J.C. Martinez, F.X. Aviles, and L. Serrano Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domain J. Mol. Biol. 283 1998 1027 1036
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 10
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • F. Chiti, N. Taddei, P.M. White, M. Bucciantini, F. Magherini, M. Stefani, and C.M. Dobson Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding Nat. Struct. Biol. 6 1999 1005 1009
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1    Taddei, N.2    White, P.M.3    Bucciantini, M.4    Magherini, F.5    Stefani, M.6    Dobson, C.M.7
  • 11
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway
    • J. Clarke, E. Cota, S.B. Fowler, and S.J. Hamill Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway Struct. Fold. Des. 7 1999 1145 1153
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 13
    • 0031792027 scopus 로고    scopus 로고
    • The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate
    • C.P.M. van Mierlo, W.M. van Dongen, F. Vergeldt, W.J. van Berkel, and E. Steensma The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate Protein Sci. 7 1998 2331 2344
    • (1998) Protein Sci. , vol.7 , pp. 2331-2344
    • Van Mierlo, C.P.M.1    Van Dongen, W.M.2    Vergeldt, F.3    Van Berkel, W.J.4    Steensma, E.5
  • 14
    • 0033980811 scopus 로고    scopus 로고
    • Apoflavodoxin (un)folding followed at the residue level by NMR
    • C.P.M. van Mierlo, J.M. van den Oever, and E. Steensma Apoflavodoxin (un)folding followed at the residue level by NMR Protein Sci. 9 2000 145 157
    • (2000) Protein Sci. , vol.9 , pp. 145-157
    • Van Mierlo, C.P.M.1    Van Den Oever, J.M.2    Steensma, E.3
  • 15
    • 4043074820 scopus 로고    scopus 로고
    • Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin
    • Y.J.M. Bollen, I.E. Sánchez, and C.P.M. van Mierlo Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin Biochemistry 43 2004 10475 10489
    • (2004) Biochemistry , vol.43 , pp. 10475-10489
    • Bollen, Y.J.M.1    Sánchez, I.E.2    Van Mierlo, C.P.M.3
  • 16
    • 0031565915 scopus 로고    scopus 로고
    • A structural census of genomes: Comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure
    • M. Gerstein A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure J. Mol. Biol. 274 1997 562 576
    • (1997) J. Mol. Biol. , vol.274 , pp. 562-576
    • Gerstein, M.1
  • 17
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G. Murzin, S.E. Brenner, T. Hubbard, and C. Chothia SCOP: a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247 1995 536 540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 18
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • W.R. Pearson Rapid and sensitive sequence comparison with FASTP and FASTA Methods Enzymol. 183 1990 63 98
    • (1990) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 19
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2
    • E. Lopez-Hernandez, and L. Serrano Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, CI-2 Fold. Des. 1 1996 43 55
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 20
    • 0031588693 scopus 로고    scopus 로고
    • Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities
    • E. Lopez-Hernandez, P. Cronet, L. Serrano, and V. Munoz Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities J. Mol. Biol. 266 1997 610 620
    • (1997) J. Mol. Biol. , vol.266 , pp. 610-620
    • Lopez-Hernandez, E.1    Cronet, P.2    Serrano, L.3    Munoz, V.4
  • 21
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • J.K. Myers, C.N. Pace, and J.M. Scholtz Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 22
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect
    • V. Munoz, E.M. Lopez, M. Jager, and L. Serrano Kinetic characterization of the chemotactic protein from Escherichia coli, CheY. Kinetic analysis of the inverse hydrophobic effect Biochemistry 33 1994 5858 5866
    • (1994) Biochemistry , vol.33 , pp. 5858-5866
    • Munoz, V.1    Lopez, E.M.2    Jager, M.3    Serrano, L.4
  • 24
    • 0035909813 scopus 로고    scopus 로고
    • Apoflavodoxin folding mechanism: An alpha/beta protein with an essentially off-pathway intermediate
    • J. Fernandez-Recio, C.G. Genzor, and J. Sancho Apoflavodoxin folding mechanism: an alpha/beta protein with an essentially off-pathway intermediate Biochemistry 40 2001 15234 15245
    • (2001) Biochemistry , vol.40 , pp. 15234-15245
    • Fernandez-Recio, J.1    Genzor, C.G.2    Sancho, J.3
  • 25
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology
    • E. Steensma, and C.P.M. van Mierlo Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology J. Mol. Biol. 282 1998 653 666
    • (1998) J. Mol. Biol. , vol.282 , pp. 653-666
    • Steensma, E.1    Van Mierlo, C.P.M.2
  • 26
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • C. Clementi, H. Nymeyer, and J.N. Onuchic Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins J. Mol. Biol. 298 2000 937 953
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 27
    • 0032847748 scopus 로고    scopus 로고
    • Elementary steps in protein folding
    • O. Bieri, and T. Kiefhaber Elementary steps in protein folding Biol. Chem. 380 1999 923 929
    • (1999) Biol. Chem. , vol.380 , pp. 923-929
    • Bieri, O.1    Kiefhaber, T.2
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis 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
  • 30
    • 0043237588 scopus 로고    scopus 로고
    • Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding
    • F. Krieger, B. Fierz, O. Bieri, M. Drewello, and T. Kiefhaber Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding J. Mol. Biol. 332 2003 265 274
    • (2003) J. Mol. Biol. , vol.332 , pp. 265-274
    • Krieger, F.1    Fierz, B.2    Bieri, O.3    Drewello, M.4    Kiefhaber, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.