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Volumn 21, Issue 7, 2013, Pages 1127-1136

Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators

Author keywords

[No Author keywords available]

Indexed keywords

BLUE LIGHT REGULATED SHK YF1; PROTEIN HISTIDINE KINASE; UNCLASSIFIED DRUG;

EID: 84879836986     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.04.024     Document Type: Article
Times cited : (163)

References (57)
  • 3
    • 34248371291 scopus 로고    scopus 로고
    • The signaling helix: A common functional theme in diverse signaling proteins
    • V. Anantharaman, S. Balaji, and L. Aravind The signaling helix: a common functional theme in diverse signaling proteins Biol. Direct 1 2006 25
    • (2006) Biol. Direct , vol.1 , pp. 25
    • Anantharaman, V.1    Balaji, S.2    Aravind, L.3
  • 5
    • 69949148703 scopus 로고    scopus 로고
    • In vivo mutational analysis of YtvA from Bacillus subtilis: Mechanism of light activation of the general stress response
    • M. Avila-Pérez, J. Vreede, Y. Tang, O. Bende, A. Losi, W. Gärtner, and K. Hellingwerf In vivo mutational analysis of YtvA from Bacillus subtilis: mechanism of light activation of the general stress response J. Biol. Chem. 284 2009 24958 24964
    • (2009) J. Biol. Chem. , vol.284 , pp. 24958-24964
    • Avila-Pérez, M.1    Vreede, J.2    Tang, Y.3    Bende, O.4    Losi, A.5    Gärtner, W.6    Hellingwerf, K.7
  • 6
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • A.M. Bilwes, L.A. Alex, B.R. Crane, and M.I. Simon Structure of CheA, a signal-transducing histidine kinase Cell 96 1999 131 141
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 7
    • 84871016428 scopus 로고    scopus 로고
    • Evolution of two-component signal transduction systems
    • E.J. Capra, and M.T. Laub Evolution of two-component signal transduction systems Annu. Rev. Microbiol. 66 2012 325 347
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 325-347
    • Capra, E.J.1    Laub, M.T.2
  • 8
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • P. Casino, V. Rubio, and A. Marina Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction Cell 139 2009 325 336
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 10
    • 59649092359 scopus 로고    scopus 로고
    • Structural analysis of ligand stimulation of the histidine kinase NarX
    • J. Cheung, and W.A. Hendrickson Structural analysis of ligand stimulation of the histidine kinase NarX Structure 17 2009 190 201
    • (2009) Structure , vol.17 , pp. 190-201
    • Cheung, J.1    Hendrickson, W.A.2
  • 13
    • 84860285553 scopus 로고    scopus 로고
    • Completion of autobuilt protein models using a database of protein fragments
    • K. Cowtan Completion of autobuilt protein models using a database of protein fragments Acta Crystallogr. D Biol. Crystallogr. 68 2012 328 335
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 328-335
    • Cowtan, K.1
  • 14
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • S. Crosson, and K. Moffat Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction Proc. Natl. Acad. Sci. USA 98 2001 2995 3000
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 15
    • 84863006375 scopus 로고    scopus 로고
    • Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis
    • A.E. Dago, A. Schug, A. Procaccini, J.A. Hoch, M. Weigt, and H. Szurmant Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis Proc. Natl. Acad. Sci. USA 109 2012 E1733 E1742
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Dago, A.E.1    Schug, A.2    Procaccini, A.3    Hoch, J.A.4    Weigt, M.5    Szurmant, H.6
  • 16
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • S. Doublié Preparation of selenomethionyl proteins for phase determination Methods Enzymol. 276 1997 523 530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 18
    • 69849086498 scopus 로고    scopus 로고
    • The piston rises again
    • J.J. Falke, and A.H. Erbse The piston rises again Structure 17 2009 1149 1151
    • (2009) Structure , vol.17 , pp. 1149-1151
    • Falke, J.J.1    Erbse, A.H.2
  • 21
    • 70349541000 scopus 로고    scopus 로고
    • Biological insights from structures of two-component proteins
    • R. Gao, and A.M. Stock Biological insights from structures of two-component proteins Annu. Rev. Microbiol. 63 2009 133 154
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 133-154
    • Gao, R.1    Stock, A.M.2
  • 22
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • A.S. Halavaty, and K. Moffat N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa Biochemistry 46 2007 14001 14009
    • (2007) Biochemistry , vol.46 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 23
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • S.M. Harper, L.C. Neil, and K.H. Gardner Structural basis of a phototropin light switch Science 301 2003 1541 1544
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 24
    • 80052968825 scopus 로고    scopus 로고
    • Function, structure and mechanism of bacterial photosensory LOV proteins
    • J. Herrou, and S. Crosson Function, structure and mechanism of bacterial photosensory LOV proteins Nat. Rev. Microbiol. 9 2011 713 723
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 713-723
    • Herrou, J.1    Crosson, S.2
  • 27
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • W. Kabsch A solution for the best rotation to relate two sets of vectors Acta Crystallogr. A 32 1976 922 923
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 29
    • 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. Cryst. 24 1991 946 950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 31
    • 84861486823 scopus 로고    scopus 로고
    • XDSAPP: A graphical user interface for the convenient processing of diffraction data using XDS
    • M. Krug, M.S. Weiss, U. Heinemann, and U. Mueller XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS J. Appl. Cryst. 45 2012 568 572
    • (2012) J. Appl. Cryst. , vol.45 , pp. 568-572
    • Krug, M.1    Weiss, M.S.2    Heinemann, U.3    Mueller, U.4
  • 32
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • A. Marina, C.D. Waldburger, and W.A. Hendrickson Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein EMBO J. 24 2005 4247 4259
    • (2005) EMBO J. , vol.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 33
    • 58549088979 scopus 로고    scopus 로고
    • In vivo generation of flavoproteins with modified cofactors
    • T. Mathes, C. Vogl, J. Stolz, and P. Hegemann In vivo generation of flavoproteins with modified cofactors J. Mol. Biol. 385 2009 1511 1518
    • (2009) J. Mol. Biol. , vol.385 , pp. 1511-1518
    • Mathes, T.1    Vogl, C.2    Stolz, J.3    Hegemann, P.4
  • 34
    • 33750459691 scopus 로고    scopus 로고
    • Dynamic helix interactions in transmembrane signaling
    • E.E. Matthews, M. Zoonens, and D.M. Engelman Dynamic helix interactions in transmembrane signaling Cell 127 2006 447 450
    • (2006) Cell , vol.127 , pp. 447-450
    • Matthews, E.E.1    Zoonens, M.2    Engelman, D.M.3
  • 36
    • 34548546911 scopus 로고    scopus 로고
    • Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA
    • A. Möglich, and K. Moffat Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA J. Mol. Biol. 373 2007 112 126
    • (2007) J. Mol. Biol. , vol.373 , pp. 112-126
    • Möglich, A.1    Moffat, K.2
  • 37
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of light-regulated histidine kinases
    • A. Möglich, R.A. Ayers, and K. Moffat Design and signaling mechanism of light-regulated histidine kinases J. Mol. Biol. 385 2009 1433 1444
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 38
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • A. Möglich, R.A. Ayers, and K. Moffat Structure and signaling mechanism of Per-ARNT-Sim domains Structure 17 2009 1282 1294
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 39
    • 77954383214 scopus 로고    scopus 로고
    • Addition at the molecular level: Signal integration in designed Per-ARNT-Sim receptor proteins
    • A. Möglich, R.A. Ayers, and K. Moffat Addition at the molecular level: signal integration in designed Per-ARNT-Sim receptor proteins J. Mol. Biol. 400 2010 477 486
    • (2010) J. Mol. Biol. , vol.400 , pp. 477-486
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 40
    • 69849100029 scopus 로고    scopus 로고
    • Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS
    • J.O. Moore, and W.A. Hendrickson Structural analysis of sensor domains from the TMAO-responsive histidine kinase receptor TorS Structure 17 2009 1195 1204
    • (2009) Structure , vol.17 , pp. 1195-1204
    • Moore, J.O.1    Hendrickson, W.A.2
  • 44
    • 84857371657 scopus 로고    scopus 로고
    • From dusk till dawn: One-plasmid systems for light-regulated gene expression
    • R. Ohlendorf, R.R. Vidavski, A. Eldar, K. Moffat, and A. Möglich From dusk till dawn: one-plasmid systems for light-regulated gene expression J. Mol. Biol. 416 2012 534 542
    • (2012) J. Mol. Biol. , vol.416 , pp. 534-542
    • Ohlendorf, R.1    Vidavski, R.R.2    Eldar, A.3    Moffat, K.4    Möglich, A.5
  • 45
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • J.S. Parkinson, and E.C. Kofoid Communication modules in bacterial signaling proteins Annu. Rev. Genet. 26 1992 71 112
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 47
    • 0027504131 scopus 로고
    • The essential tension: Opposed reactions in bacterial two-component regulatory systems
    • F.D. Russo, and T.J. Silhavy The essential tension: opposed reactions in bacterial two-component regulatory systems Trends Microbiol. 1 1993 306 310
    • (1993) Trends Microbiol. , vol.1 , pp. 306-310
    • Russo, F.D.1    Silhavy, T.J.2
  • 48
    • 0001841380 scopus 로고
    • On the rigid-body motion of molecules in crystals
    • V. Schomaker, and K.N. Trueblood On the rigid-body motion of molecules in crystals Acta Crystallogr. B 24 1968 63 76
    • (1968) Acta Crystallogr. B , vol.24 , pp. 63-76
    • Schomaker, V.1    Trueblood, K.N.2
  • 50
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • G.M. Sheldrick A short history of SHELX Acta Crystallogr. A 64 2008 112 122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 51
    • 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
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • H. Szurmant, R.A. White, and J.A. Hoch Sensor complexes regulating two-component signal transduction Curr. Opin. Struct. Biol. 17 2007 706 715
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 55
    • 84874684844 scopus 로고    scopus 로고
    • Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains
    • C. Wang, J. Sang, J. Wang, M. Su, J.S. Downey, Q. Wu, S. Wang, Y. Cai, X. Xu, and J. Wu Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains PLoS Biol. 11 2013 e1001493
    • (2013) PLoS Biol. , vol.11 , pp. 1001493
    • Wang, C.1    Sang, J.2    Wang, J.3    Su, M.4    Downey, J.S.5    Wu, Q.6    Wang, S.7    Cai, Y.8    Xu, X.9    Wu, J.10
  • 57
    • 55749108880 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction
    • X. Yang, J. Kuk, and K. Moffat Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction Proc. Natl. Acad. Sci. USA 105 2008 14715 14720
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14715-14720
    • Yang, X.1    Kuk, J.2    Moffat, K.3


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