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Volumn 22, Issue 5, 2013, Pages 557-563

A conserved threonine spring-loads precursor for intein splicing

Author keywords

Autocatalytic proteins; Crystal structure; First principles quantum mechanics; Intein; Reaction rate

Indexed keywords

EXTEIN; INTEIN; THREONINE;

EID: 84962383339     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2236     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0025226104 scopus 로고
    • +-adenosine triphosphatase
    • Kane PM, Yamashiro CT, Wolczyk DF, Neff N, Goebl M, Stevens TH (1990) Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase. Science 250: 651-657. (Pubitemid 120034281)
    • (1990) Science , vol.250 , Issue.4981 , pp. 651-657
    • Kane, P.M.1    Yamashiro, C.T.2    Wolczyk, D.F.3    Neff, N.4    Goebl, M.5    Stevens, T.H.6
  • 2
    • 0025240361 scopus 로고
    • Molecular-structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine-triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • Hirata R, Ohsumi Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (1990) Molecular-structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine-triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J Biol Chem 265: 6726-6733.
    • (1990) J Biol Chem , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumi, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 3
    • 0032498234 scopus 로고    scopus 로고
    • Protein splicing of inteins and hedgehog autoproteolysis: Structure, function, and evolution
    • DOI 10.1016/S0092-8674(00)80892-2
    • Perler FB (1998) Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell 92: 1-4. (Pubitemid 28053291)
    • (1998) Cell , vol.92 , Issue.1 , pp. 1-4
    • Perler, F.B.1
  • 4
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus H (2000) Protein splicing and related forms of protein autoprocessing. Ann Rev Biochem 69: 447-496.
    • (2000) Ann Rev Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 5
    • 80051707071 scopus 로고    scopus 로고
    • Amide bonds to the nitrogen atoms of cysteine and serine as "weak points" in the backbones of proteins
    • Lewis CA, Jr, Wolfenden R (2011) Amide bonds to the nitrogen atoms of cysteine and serine as "weak points" in the backbones of proteins. Biochemistry 50: 7259-7264.
    • (2011) Biochemistry , vol.50 , pp. 7259-7264
    • Lewis Jr., C.A.1    Wolfenden, R.2
  • 6
    • 79955619798 scopus 로고    scopus 로고
    • Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications
    • Callahan BP, Topilina NI, Stanger MJ, Van Roey P, Belfort M (2011) Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications. Nat Struct Mol Biol 18: 630-633.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 630-633
    • Callahan, B.P.1    Topilina, N.I.2    Stanger, M.J.3    Van Roey, P.4    Belfort, M.5
  • 7
    • 0033520327 scopus 로고    scopus 로고
    • Structural insights into the mechanism of intramolecular proteolysis
    • DOI 10.1016/S0092-8674(00)80052-5
    • Xu Q, Buckley D, Guan C, Guo HC (1999) Structural insights into the mechanism of intramolecular proteolysis. Cell 98: 651-661. (Pubitemid 29418956)
    • (1999) Cell , vol.98 , Issue.5 , pp. 651-661
    • Xu, Q.1    Buckley, D.2    Guan, C.3    Guo, H.-C.4
  • 8
    • 0034595699 scopus 로고    scopus 로고
    • Structural insights into the protein splicing mechanism of PI-SceI
    • DOI 10.1074/jbc.275.22.16408
    • Poland B, Xu MQ, Quiocho FA (2000) Structural insights into the protein splicing mechanism of Pl-Scel. J Biol Chem 275: 16408-16413. (Pubitemid 30398859)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16408-16413
    • Poland, B.W.1    Xu, M.-Q.2    Quiocho, F.A.3
  • 10
    • 67650480533 scopus 로고    scopus 로고
    • Protein autoproteolysis: Conformational strain linked to the rate of peptide cleavage by the pH dependence of the N-> O acyl shift reaction
    • Johansson DG A, Wallin G, Sandberg A, Macao B, Åqvist J, Härd T (2009) Protein autoproteolysis: conformational strain linked to the rate of peptide cleavage by the pH dependence of the N-> O acyl shift reaction. J Am Chem Soc 131: 9475-9477.
    • (2009) J Am Chem Soc , vol.131 , pp. 9475-9477
    • Johansson, D.G.A.1    Wallin, G.2    Sandberg, A.3    MacAo, B.4    Åqvist, J.5    Härd, T.6
  • 11
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • DOI 10.1038/nsb0198-31
    • Klabunde T, Sharma S, Telenti A, Jacobs WR, Jr, Sacchettini JC (1998) Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nat Struct Biol 5: 31-36. (Pubitemid 28048974)
    • (1998) Nature Structural Biology , vol.5 , Issue.1 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 15
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The intein database
    • Perler FB (2002) InBase: the intein database. Nucleic Acids Res 30: 383-384.
    • (2002) Nucleic Acids Res , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 16
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette PH, Aslund F, Beckwith J, Georgiou G (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci USA 96: 13703-13708.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 17
    • 70349446285 scopus 로고    scopus 로고
    • Protein splicing: A versatile tool for drug discovery
    • Cheriyan M, Perler FB (2009) Protein splicing: a versatile tool for drug discovery. Adv Drug Del Rev 61: 899-907.
    • (2009) Adv Drug Del Rev , vol.61 , pp. 899-907
    • Cheriyan, M.1    Perler, F.B.2
  • 18
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing
    • Vila-Perello M, Muir TW (2010) Biological applications of protein splicing. Cell 143: 191-200.
    • (2010) Cell , vol.143 , pp. 191-200
    • Vila-Perello, M.1    Muir, T.W.2
  • 19
    • 84876750534 scopus 로고    scopus 로고
    • A redox trap to augment the intein toolbox
    • in press doi: 10.1002/bit.24821
    • Callahan BP, Stanger M, Belfort M (in press) A redox trap to augment the intein toolbox. Biotechnol Bioeng. doi: 10.1002/bit.24821.
    • Biotechnol Bioeng.
    • Callahan, B.P.1    Stanger, M.2    Belfort, M.3
  • 20
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke AD (1993) Density-functional thermochemistry. III. The role of exact exchange. J ChemPhys 98: 5648-5642.
    • (1993) J ChemPhys , vol.98 , pp. 5648-5642
    • Becke, A.D.1
  • 21
    • 84986527758 scopus 로고
    • IMOMM -A new integrated ab-initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition-states
    • Maseras F, Morokuma K (1995) IMOMM -a new integrated ab-initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition-states. J Comput Chem 16: 1170-1179.
    • (1995) J Comput Chem , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 24
    • 85005693478 scopus 로고
    • Combining synchronous transit and quasi-Newton methods to find transitionstates
    • Peng C, Schlegel HB (1993) Combining synchronous transit and quasi-Newton methods to find transitionstates. Isr J Chem 33: 449-454.
    • (1993) Isr J Chem , vol.33 , pp. 449-454
    • Peng, C.1    Schlegel, H.B.2
  • 25
    • 2442481958 scopus 로고    scopus 로고
    • Using redundant internal coordinates to optimize equilibrium geometries and transition states
    • Peng C, Ayala PY, Schlegel HB, Frisch MJ (1996) Using redundant internal coordinates to optimize equilibrium geometries and transition states. J Comput Chem 17: 49-56. (Pubitemid 126581859)
    • (1996) Journal of Computational Chemistry , vol.17 , Issue.1 , pp. 49-56
    • Peng, C.1    Ayala, P.Y.2    Schlegel, H.B.3    Frisch, M.J.4
  • 26
    • 84946893847 scopus 로고
    • Electrostatic interaction of a solute with a continuum -A direct utilization of ab initio molecular potentials for the prevision of solvent effects
    • Miertus S, Scrocco E, Tomasi J (1981) Electrostatic interaction of a solute with a continuum -a direct utilization of ab initio molecular potentials for the prevision of solvent effects. J Chem Phys 55: 117-129.
    • (1981) J Chem Phys , vol.55 , pp. 117-129
    • Miertus, S.1    Scrocco, E.2    Tomasi, J.3
  • 27
    • 0035451052 scopus 로고    scopus 로고
    • What are the dielectric "constants" of proteins and how to validate electrostatic models?
    • DOI 10.1002/prot.1106
    • Schutz CN, Warshel A (2001) What are the dielectric "constants" of proteins and how to validate electrostatic models? Proteins 44: 400-417. (Pubitemid 32768578)
    • (2001) Proteins: Structure, Function and Genetics , vol.44 , Issue.4 , pp. 400-417
    • Schutz, C.N.1    Warshel, A.2
  • 28
    • 0000405834 scopus 로고    scopus 로고
    • Solvation dynamics in protein environments studied by photon echo spectroscopy
    • Jordanides XJ, Lang MJ, Song X, Fleming GR (1999) Solvation dynamics in protein environments studied by photon echo spectroscopy. J Phys Chem B 103: 7995-8005.
    • (1999) J Phys Chem B , vol.103 , pp. 7995-8005
    • Jordanides, X.J.1    Lang, M.J.2    Song, X.3    Fleming, G.R.4
  • 29
    • 33748898492 scopus 로고    scopus 로고
    • Different types of biological proton transfer reactions studied by quantum chemical methods
    • DOI 10.1016/j.bbabio.2006.01.002, PII S000527280600003X
    • Blomberg MRA, Siegbahn PEM (2006) Different types of biological proton transfer reactions studied by quantum chemical methods. Biochim Biophys Acta 1757: 969-980. (Pubitemid 44427751)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.8 , pp. 969-980
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2
  • 30
    • 77349101326 scopus 로고    scopus 로고
    • Reflections on protein splicing: Structures, functions, and mechanisms
    • Anraku Y, Satow Y (2009) Reflections on protein splicing: structures, functions, and mechanisms. Proc Jpn Acad Ser B 85: 409-421.
    • (2009) Proc Jpn Acad ser B , vol.85 , pp. 409-421
    • Anraku, Y.1    Satow, Y.2
  • 31
    • 0032359384 scopus 로고    scopus 로고
    • The chemical basis of protein splicing
    • Paulus H (1998) The chemical basis of protein splicing. Chem Rev 27: 375-386.
    • (1998) Chem Rev , vol.27 , pp. 375-386
    • Paulus, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.