메뉴 건너뛰기




Volumn 30, Issue 5, 2008, Pages 642-648

Knotted Fusion Proteins Reveal Unexpected Possibilities in Protein Folding

Author keywords

PROTEINS

Indexed keywords

AMINO ACID; CARBOXYL GROUP; HOMODIMER; HYBRID PROTEIN; PROTEIN SUBUNIT;

EID: 44449146446     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.03.019     Document Type: Article
Times cited : (62)

References (35)
  • 1
    • 0037526102 scopus 로고    scopus 로고
    • Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition
    • Ahn H.J., Kim H.W., Yoon H.J., Lee B.I., Suh S.W., and Yang J.K. Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. EMBO J. 22 (2003) 2593-2603
    • (2003) EMBO J. , vol.22 , pp. 2593-2603
    • Ahn, H.J.1    Kim, H.W.2    Yoon, H.J.3    Lee, B.I.4    Suh, S.W.5    Yang, J.K.6
  • 5
    • 0037133505 scopus 로고    scopus 로고
    • The N-terminal extension of rusticyanin is not responsible for its acid stability
    • Grossmann J.G., Hall J.F., Kanbi L.D., and Hasnain S.S. The N-terminal extension of rusticyanin is not responsible for its acid stability. Biochemistry 41 (2002) 3613-3619
    • (2002) Biochemistry , vol.41 , pp. 3613-3619
    • Grossmann, J.G.1    Hall, J.F.2    Kanbi, L.D.3    Hasnain, S.S.4
  • 6
    • 0033613816 scopus 로고    scopus 로고
    • Engineered assembly of intertwined oligomers of an immunoglobulin domain
    • Hayes M.V., Sessions R.L.B., and Clarke A.R. Engineered assembly of intertwined oligomers of an immunoglobulin domain. J. Mol. Biol. 285 (1999) 1857-1867
    • (1999) J. Mol. Biol. , vol.285 , pp. 1857-1867
    • Hayes, M.V.1    Sessions, R.L.B.2    Clarke, A.R.3
  • 7
    • 0023058914 scopus 로고
    • Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine
    • Hoffman J.L. Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine. Biochemistry 25 (1986) 4444-4449
    • (1986) Biochemistry , vol.25 , pp. 4444-4449
    • Hoffman, J.L.1
  • 8
    • 34547563369 scopus 로고    scopus 로고
    • Protein knot server: detection of knots in protein structures
    • Kolesov G., Virnau P., Kardar M., and Mirny L.A. Protein knot server: detection of knots in protein structures. Nucleic Acids Res. 35 (2007) W425-W428
    • (2007) Nucleic Acids Res. , vol.35
    • Kolesov, G.1    Virnau, P.2    Kardar, M.3    Mirny, L.A.4
  • 9
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Cryst. 34 (2001) 33-41
    • (2001) J. Appl. Cryst. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 11
    • 13844255609 scopus 로고    scopus 로고
    • Folding studies on a knotted protein
    • Mallam A.L., and Jackson S.E. Folding studies on a knotted protein. J. Mol. Biol. 346 (2005) 1409-1421
    • (2005) J. Mol. Biol. , vol.346 , pp. 1409-1421
    • Mallam, A.L.1    Jackson, S.E.2
  • 12
    • 33745163582 scopus 로고    scopus 로고
    • Probing Nature's knots: The folding pathway of a knotted homodimeric protein
    • Mallam A.L., and Jackson S.E. Probing Nature's knots: The folding pathway of a knotted homodimeric protein. J. Mol. Biol. 359 (2006) 1420-1436
    • (2006) J. Mol. Biol. , vol.359 , pp. 1420-1436
    • Mallam, A.L.1    Jackson, S.E.2
  • 13
    • 33846362515 scopus 로고    scopus 로고
    • A comparison of the folding of two knotted proteins: YbeA and YibK
    • Mallam A.L., and Jackson S.E. A comparison of the folding of two knotted proteins: YbeA and YibK. J. Mol. Biol. 366 (2007) 650-665
    • (2007) J. Mol. Biol. , vol.366 , pp. 650-665
    • Mallam, A.L.1    Jackson, S.E.2
  • 14
    • 33846099591 scopus 로고    scopus 로고
    • The dimerization of an α/β-knotted protein is essential for structure and function
    • Mallam A.L., and Jackson S.E. The dimerization of an α/β-knotted protein is essential for structure and function. Structure 15 (2007) 111-122
    • (2007) Structure , vol.15 , pp. 111-122
    • Mallam, A.L.1    Jackson, S.E.2
  • 17
    • 9644281537 scopus 로고    scopus 로고
    • Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes
    • Mosbacher T.G., Bechthold A., and Schulz G.E. Structure and function of the antibiotic resistance-mediating methyltransferase AviRb from Streptomyces viridochromogenes. J. Mol. Biol. 345 (2005) 535-545
    • (2005) J. Mol. Biol. , vol.345 , pp. 535-545
    • Mosbacher, T.G.1    Bechthold, A.2    Schulz, G.E.3
  • 18
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., and Scholtz J.M. 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
  • 19
    • 1842607227 scopus 로고    scopus 로고
    • Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
    • Nureki O., Watanabe K., Fukai S., Ishii R., Endo Y., Hori H., and Yokoyama S. Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme. Structure 12 (2004) 593-602
    • (2004) Structure , vol.12 , pp. 593-602
    • Nureki, O.1    Watanabe, K.2    Fukai, S.3    Ishii, R.4    Endo, Y.5    Hori, H.6    Yokoyama, S.7
  • 20
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 21
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 22
    • 36749095666 scopus 로고    scopus 로고
    • Spontaneous knotting of an agitated string
    • Raymer D.M., and Smith D.E. Spontaneous knotting of an agitated string. Proc. Natl. Acad. Sci. USA 104 (2007) 16432-16437
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16432-16437
    • Raymer, D.M.1    Smith, D.E.2
  • 23
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau F., Schymkowitz J.W.H., Wilkinson H.R., and Itzhaki L.S. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl. Acad. Sci. USA 98 (2001) 5596-5601
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 24
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • Rousseau F., Schymkowitz J.W.H., and Itzhaki L.S. The unfolding story of three-dimensional domain swapping. Structure 11 (2003) 243-251
    • (2003) Structure , vol.11 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Itzhaki, L.S.3
  • 26
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25 (1992) 495-503
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 27
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 28
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor W.R. A deeply knotted protein structure and how it might fold. Nature 406 (2000) 916-919
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 29
    • 34248570354 scopus 로고    scopus 로고
    • Protein knots and fold complexity: some new twists
    • Taylor W.R. Protein knots and fold complexity: some new twists. Comput. Biol. Chem. 31 (2007) 151-162
    • (2007) Comput. Biol. Chem. , vol.31 , pp. 151-162
    • Taylor, W.R.1
  • 30
    • 0037413604 scopus 로고    scopus 로고
    • Protein knots: A tangled problem
    • Taylor W.R., and Lin K. Protein knots: A tangled problem. Nature 421 (2003) 25
    • (2003) Nature , vol.421 , pp. 25
    • Taylor, W.R.1    Lin, K.2
  • 31
    • 27544511752 scopus 로고    scopus 로고
    • Knots in globule and coil phases of a model polyethylene
    • Virnau P., Kantor Y., and Kardar M. Knots in globule and coil phases of a model polyethylene. J. Am. Chem. Soc. 127 (2005) 15102-15106
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15102-15106
    • Virnau, P.1    Kantor, Y.2    Kardar, M.3
  • 32
    • 33749347406 scopus 로고    scopus 로고
    • Intricate Knots in Proteins: Function and Evolution
    • 10.1371/journal.pcbi.0020122
    • Virnau P., Mirny L.A., and Kardar M. Intricate Knots in Proteins: Function and Evolution. PLoS Comput. Biol. 2 (2006) e122 10.1371/journal.pcbi.0020122
    • (2006) PLoS Comput. Biol. , vol.2
    • Virnau, P.1    Mirny, L.A.2    Kardar, M.3
  • 33
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Cryst. 36 (2003) 860-864
    • (2003) J. Appl. Cryst. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 35
    • 36549032188 scopus 로고    scopus 로고
    • Knotted and topologically complex proteins as models for studying folding and stability
    • Yeates T.O., Norcross T.S., and King N.P. Knotted and topologically complex proteins as models for studying folding and stability. Curr. Opin. Chem. Biol. 11 (2007) 1-9
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 1-9
    • Yeates, T.O.1    Norcross, T.S.2    King, N.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.