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Volumn 22, Issue 10, 2014, Pages 1433-1445

Transient dimerization of human MxA promotes GTP hydrolysis, resulting in a mechanical power stroke

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MONOMER; MYXOVIRUS RESISTANCE PROTEIN A; NUCLEOTIDE; MX1 PROTEIN, HUMAN; MYXOVIRUS RESISTANCE PROTEIN; PROLINE;

EID: 84908177291     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.08.015     Document Type: Article
Times cited : (37)

References (58)
  • 1
    • 0037077224 scopus 로고    scopus 로고
    • The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum
    • M.A. Accola, B. Huang, A. Al Masri, and M.A. McNiven The antiviral dynamin family member, MxA, tubulates lipids and localizes to the smooth endoplasmic reticulum J. Biol. Chem. 277 2002 21829 21835
    • (2002) J. Biol. Chem. , vol.277 , pp. 21829-21835
    • Accola, M.A.1    Huang, B.2    Al Masri, A.3    McNiven, M.A.4
  • 2
    • 0027419771 scopus 로고
    • The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
    • J.A. Ali, A.P. Jackson, A.J. Howells, and A. Maxwell The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs Biochemistry 32 1993 2717 2724
    • (1993) Biochemistry , vol.32 , pp. 2717-2724
    • Ali, J.A.1    Jackson, A.P.2    Howells, A.J.3    Maxwell, A.4
  • 4
    • 79952298783 scopus 로고    scopus 로고
    • Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A
    • L.J. Byrnes, and H. Sondermann Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A Proc. Natl. Acad. Sci. USA 108 2011 2216 2221
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2216-2221
    • Byrnes, L.J.1    Sondermann, H.2
  • 6
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • J.S. Chappie, S. Acharya, M. Leonard, S.L. Schmid, and F. Dyda G domain dimerization controls dynamin's assembly-stimulated GTPase activity Nature 465 2010 435 440
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 8
    • 84880679646 scopus 로고    scopus 로고
    • Building a fission machine - Structural insights into dynamin assembly and activation
    • J.S. Chappie, and F. Dyda Building a fission machine - structural insights into dynamin assembly and activation J. Cell Sci. 126 2013 2773 2784
    • (2013) J. Cell Sci. , vol.126 , pp. 2773-2784
    • Chappie, J.S.1    Dyda, F.2
  • 9
    • 84947318637 scopus 로고
    • Locally weighted regression - An approach to regression-analysis by local fitting
    • W.S. Cleveland, and S.J. Devlin Locally weighted regression - an approach to regression-analysis by local fitting J. Am. Stat. Assoc. 83 1988 596 610
    • (1988) J. Am. Stat. Assoc. , vol.83 , pp. 596-610
    • Cleveland, W.S.1    Devlin, S.J.2
  • 14
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • M.G.J. Ford, S. Jenni, and J. Nunnari The crystal structure of dynamin Nature 477 2011 561 566
    • (2011) Nature , vol.477 , pp. 561-566
    • Ford, M.G.J.1    Jenni, S.2    Nunnari, J.3
  • 15
    • 0010394149 scopus 로고
    • Approaches that can be used with enzymes
    • C. Frieden, L.W. Nichol, John Wiley and Sons New Jersey
    • C. Frieden Approaches that can be used with enzymes C. Frieden, L.W. Nichol, Protein-Protein Interactions 1981 John Wiley and Sons New Jersey 289 314
    • (1981) Protein-Protein Interactions , pp. 289-314
    • Frieden, C.1
  • 18
    • 80755153638 scopus 로고    scopus 로고
    • Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function
    • S. Gao, A. von der Malsburg, A. Dick, K. Faelber, G.F. Schröder, O. Haller, G. Kochs, and O. Daumke Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function Immunity 35 2011 514 525
    • (2011) Immunity , vol.35 , pp. 514-525
    • Gao, S.1    Von Der Malsburg, A.2    Dick, A.3    Faelber, K.4    Schröder, G.F.5    Haller, O.6    Kochs, G.7    Daumke, O.8
  • 19
    • 84972492387 scopus 로고
    • Inference from iterative simulation using multiple sequences
    • A. Gelman, and D.B. Rubin Inference from iterative simulation using multiple sequences Stat. Sci. 7 1992 457 472
    • (1992) Stat. Sci. , vol.7 , pp. 457-472
    • Gelman, A.1    Rubin, D.B.2
  • 20
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
    • A. Ghosh, G.J.K. Praefcke, L. Renault, A. Wittinghofer, and C. Herrmann How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP Nature 440 2006 101 104
    • (2006) Nature , vol.440 , pp. 101-104
    • Ghosh, A.1    Praefcke, G.J.K.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 21
    • 77953846336 scopus 로고    scopus 로고
    • Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes
    • M. Goličnik Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes Acta Chim. Slov. 57 2010 272 287
    • (2010) Acta Chim. Slov. , vol.57 , pp. 272-287
    • Goličnik, M.1
  • 23
    • 78651515640 scopus 로고    scopus 로고
    • Human MxA protein: An interferon-induced dynamin-like GTPase with broad antiviral activity
    • O. Haller, and G. Kochs Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity J. Interferon Cytokine Res. 31 2011 79 87
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 79-87
    • Haller, O.1    Kochs, G.2
  • 24
    • 77956890234 scopus 로고
    • Monte carlo sampling methods using Markov chains and their applications
    • W.K. Hastings Monte carlo sampling methods using Markov chains and their applications Biometrika 57 1970 97 109
    • (1970) Biometrika , vol.57 , pp. 97-109
    • Hastings, W.K.1
  • 26
    • 84906311450 scopus 로고    scopus 로고
    • The large GTPase Mx1 is involved in apical transport of MDCK cells
    • F. Hoff, C. Greb, C. Hollmann, E. Hönig, and R. Jacob The large GTPase Mx1 is involved in apical transport of MDCK cells Traffic 15 2014 983 996
    • (2014) Traffic , vol.15 , pp. 983-996
    • Hoff, F.1    Greb, C.2    Hollmann, C.3    Hönig, E.4    Jacob, R.5
  • 27
    • 0026762397 scopus 로고
    • Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins
    • M.A. Horisberger Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins J. Virol. 66 1992 4705 4709
    • (1992) J. Virol. , vol.66 , pp. 4705-4709
    • Horisberger, M.A.1
  • 29
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae)
    • G. Kochs, and O. Haller GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae) J. Biol. Chem. 274 1999 4370 4376
    • (1999) J. Biol. Chem. , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 30
    • 0037134425 scopus 로고    scopus 로고
    • Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers
    • G. Kochs, M. Haener, U. Aebi, and O. Haller Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers J. Biol. Chem. 277 2002 14172 14176
    • (2002) J. Biol. Chem. , vol.277 , pp. 14172-14176
    • Kochs, G.1    Haener, M.2    Aebi, U.3    Haller, O.4
  • 31
    • 0037022575 scopus 로고    scopus 로고
    • Antivirally active MxA protein sequesters la Crosse virus nucleocapsid protein into perinuclear complexes
    • G. Kochs, C. Janzen, H. Hohenberg, and O. Haller Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes Proc. Natl. Acad. Sci. USA 99 2002 3153 3158
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3153-3158
    • Kochs, G.1    Janzen, C.2    Hohenberg, H.3    Haller, O.4
  • 32
    • 30544454966 scopus 로고    scopus 로고
    • Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1)
    • S. Kunzelmann, G.J.K. Praefcke, and C. Herrmann Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1) Methods Enzymol. 404 2005 512 527
    • (2005) Methods Enzymol. , vol.404 , pp. 512-527
    • Kunzelmann, S.1    Praefcke, G.J.K.2    Herrmann, C.3
  • 33
  • 34
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • G. Langer, S.X. Cohen, V.S. Lamzin, and A. Perrakis Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3 2008 1171 1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 37
    • 0028007455 scopus 로고
    • Mutational analysis of murine Mx1 protein: GTP binding core domain is essential for anti-influenza A activity
    • K. Melén, and I. Julkunen Mutational analysis of murine Mx1 protein: GTP binding core domain is essential for anti-influenza A activity Virology 205 1994 269 279
    • (1994) Virology , vol.205 , pp. 269-279
    • Melén, K.1    Julkunen, I.2
  • 39
    • 84867659115 scopus 로고    scopus 로고
    • Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA
    • P.S. Mitchell, C. Patzina, M. Emerman, O. Haller, H.S. Malik, and G. Kochs Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA Cell Host Microbe 12 2012 598 604
    • (2012) Cell Host Microbe , vol.12 , pp. 598-604
    • Mitchell, P.S.1    Patzina, C.2    Emerman, M.3    Haller, O.4    Malik, H.S.5    Kochs, G.6
  • 40
    • 84882883270 scopus 로고    scopus 로고
    • An evolutionary perspective on the broad antiviral specificity of MxA
    • P.S. Mitchell, M. Emerman, and H.S. Malik An evolutionary perspective on the broad antiviral specificity of MxA Curr. Opin. Microbiol. 16 2013 493 499
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 493-499
    • Mitchell, P.S.1    Emerman, M.2    Malik, H.S.3
  • 41
    • 84877781381 scopus 로고    scopus 로고
    • Mechanics of dynamin-mediated membrane fission
    • S. Morlot, and A. Roux Mechanics of dynamin-mediated membrane fission Annu Rev Biophys 42 2013 629 649
    • (2013) Annu Rev Biophys , vol.42 , pp. 629-649
    • Morlot, S.1    Roux, A.2
  • 43
    • 0035503309 scopus 로고    scopus 로고
    • Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
    • H.H. Niemann, M.L. Knetsch, A. Scherer, D.J. Manstein, and F.J. Kull Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms EMBO J. 20 2001 5813 5821
    • (2001) EMBO J. , vol.20 , pp. 5813-5821
    • Niemann, H.H.1    Knetsch, M.L.2    Scherer, A.3    Manstein, D.J.4    Kull, F.J.5
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 84896877632 scopus 로고    scopus 로고
    • Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus
    • C. Patzina, O. Haller, and G. Kochs Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus J. Biol. Chem. 289 2014 6020 6027
    • (2014) J. Biol. Chem. , vol.289 , pp. 6020-6027
    • Patzina, C.1    Haller, O.2    Kochs, G.3
  • 46
    • 0000578552 scopus 로고
    • Multiple intermediates in steady state enzyme kinetics. I. The mechanism involving a single substrate and product
    • L. Peller, and R.A. Alberty Multiple intermediates in steady state enzyme kinetics. I. The mechanism involving a single substrate and product J. Am. Chem. Soc. 81 1959 5907 5914
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 5907-5914
    • Peller, L.1    Alberty, R.A.2
  • 49
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • B. Prakash, G.J. Praefcke, L. Renault, A. Wittinghofer, and C. Herrmann Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins Nature 403 2000 567 571
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 51
    • 0028854181 scopus 로고
    • Vesicular stomatitis virus transcription inhibited by purified MxA protein
    • M. Schwemmle, K.C. Weining, M.F. Richter, B. Schumacher, and P. Staeheli Vesicular stomatitis virus transcription inhibited by purified MxA protein Virology 206 1995 545 554
    • (1995) Virology , vol.206 , pp. 545-554
    • Schwemmle, M.1    Weining, K.C.2    Richter, M.F.3    Schumacher, B.4    Staeheli, P.5
  • 52
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: A program for mutating pdb files used as templates in molecular replacement
    • N. Stein CHAINSAW: a program for mutating pdb files used as templates in molecular replacement J. Appl. Cryst. 41 2008 641 643
    • (2008) J. Appl. Cryst. , vol.41 , pp. 641-643
    • Stein, N.1
  • 53
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • T.W. Traut Physiological concentrations of purines and pyrimidines Mol. Cell. Biochem. 140 1994 1 22
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 54
    • 84890476408 scopus 로고    scopus 로고
    • Mx proteins: Antiviral gatekeepers that restrain the uninvited
    • J. Verhelst, P. Hulpiau, and X. Saelens Mx proteins: antiviral gatekeepers that restrain the uninvited Microbiol. Mol. Biol. Rev. 77 2013 551 566
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 551-566
    • Verhelst, J.1    Hulpiau, P.2    Saelens, X.3
  • 55
    • 80054828458 scopus 로고    scopus 로고
    • Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop
    • A. von der Malsburg, I. Abutbul-Ionita, O. Haller, G. Kochs, and D. Danino Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop J. Biol. Chem. 286 2011 37858 37865
    • (2011) J. Biol. Chem. , vol.286 , pp. 37858-37865
    • Von Der Malsburg, A.1    Abutbul-Ionita, I.2    Haller, O.3    Kochs, G.4    Danino, D.5
  • 56
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • D.E. Warnock, J.E. Hinshaw, and S.L. Schmid Dynamin self-assembly stimulates its GTPase activity J. Biol. Chem. 271 1996 22310 22314
    • (1996) J. Biol. Chem. , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 58
    • 83455178069 scopus 로고    scopus 로고
    • Structural basis for mechanochemical role of Arabidopsis thaliana dynamin-related protein in membrane fission
    • L. Yan, Y. Ma, Y. Sun, J. Gao, X. Chen, J. Liu, C. Wang, Z. Rao, and Z. Lou Structural basis for mechanochemical role of Arabidopsis thaliana dynamin-related protein in membrane fission J. Mol. Cell Biol. 3 2011 378 381
    • (2011) J. Mol. Cell Biol. , vol.3 , pp. 378-381
    • Yan, L.1    Ma, Y.2    Sun, Y.3    Gao, J.4    Chen, X.5    Liu, J.6    Wang, C.7    Rao, Z.8    Lou, Z.9


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