메뉴 건너뛰기




Volumn 342, Issue 3, 2004, Pages 953-970

Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches

Author keywords

conformational switch; crystal structure; FtsZ; G protein; tubulin

Indexed keywords

ALPHA TUBULIN; BACTERIAL PROTEIN; BETA TUBULIN; CITRIC ACID; FTSZ PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE;

EID: 4444349738     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.061     Document Type: Article
Times cited : (108)

References (53)
  • 2
    • 0036019535 scopus 로고    scopus 로고
    • The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis
    • S.G. Addinall, and B. Holland The tubulin ancestor, FtsZ, draughtsman, designer and driving force for bacterial cytokinesis J. Mol. Biol. 318 2002 219 236
    • (2002) J. Mol. Biol. , vol.318 , pp. 219-236
    • Addinall, S.G.1    Holland, B.2
  • 4
    • 0345600249 scopus 로고    scopus 로고
    • The division of endosymbiotic organelles
    • K.W. Osteryoung, and J. Nunnari The division of endosymbiotic organelles Science 302 2003 1698 1704
    • (2003) Science , vol.302 , pp. 1698-1704
    • Osteryoung, K.W.1    Nunnari, J.2
  • 6
    • 0242582382 scopus 로고    scopus 로고
    • Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics
    • J. Wang, A. Galgoci, S. Kodali, K.B. Herath, H. Jayasuriya, and K. Dorso Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics J. Biol. Chem. 278 2003 44424 44428
    • (2003) J. Biol. Chem. , vol.278 , pp. 44424-44428
    • Wang, J.1    Galgoci, A.2    Kodali, S.3    Herath, K.B.4    Jayasuriya, H.5    Dorso, K.6
  • 9
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • E. Nogales, S.G. Wolf, and K.H. Downing Structure of the alpha beta tubulin dimer by electron crystallography Nature 391 1998 199 203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 10
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 a resolution
    • J. Lowe, H. Li, K.H. Downing, and E. Nogales Refined structure of alpha beta-tubulin at 3.5 A resolution J. Mol. Biol. 313 2001 1045 1057
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 11
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • J. Lowe, and L.A. Amos Crystal structure of the bacterial cell-division protein FtsZ Nature 391 1998 203 206
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 12
    • 0038610624 scopus 로고    scopus 로고
    • Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ
    • S.C. Cordell, E.J. Robinson, and J. Lowe Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ Proc. Natl Acad. Sci. USA 100 2003 7889 7894
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7889-7894
    • Cordell, S.C.1    Robinson, E.J.2    Lowe, J.3
  • 13
    • 0037495314 scopus 로고    scopus 로고
    • Tubulin-like protofilaments in Ca2+-induced FtsZ sheets
    • J. Lowe, and L.A. Amos Tubulin-like protofilaments in Ca2+-induced FtsZ sheets EMBO J. 18 1999 2364 2371
    • (1999) EMBO J. , vol.18 , pp. 2364-2371
    • Lowe, J.1    Amos, L.A.2
  • 14
    • 0030931117 scopus 로고    scopus 로고
    • Analysis of the interaction of FtsZ with itself, GTP, and FtsA
    • X. Wang, J. Huang, A. Mukherjee, C. Cao, and J. Lutkenhaus Analysis of the interaction of FtsZ with itself, GTP, and FtsA J. Bacteriol. 179 1997 5551 5559
    • (1997) J. Bacteriol. , vol.179 , pp. 5551-5559
    • Wang, X.1    Huang, J.2    Mukherjee, A.3    Cao, C.4    Lutkenhaus, J.5
  • 15
    • 0031914188 scopus 로고    scopus 로고
    • Atomic structures of tubulin and FtsZ
    • H.P. Erickson Atomic structures of tubulin and FtsZ Trends Cell Biol. 8 1998 133 137
    • (1998) Trends Cell Biol. , vol.8 , pp. 133-137
    • Erickson, H.P.1
  • 16
    • 0034517639 scopus 로고    scopus 로고
    • Crystallization of the Mycobacterium tuberculosis cell-division protein FtsZ
    • A.K. Leung, E.L. White, L.J. Ross, and D.W. Borhani Crystallization of the Mycobacterium tuberculosis cell-division protein FtsZ Acta Crystallog. sect. D 56 2000 1634 1637
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 1634-1637
    • Leung, A.K.1    White, E.L.2    Ross, L.J.3    Borhani, D.W.4
  • 19
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • J. Janin, and F. Rodier Protein-protein interaction at crystal contacts Proteins: Struct. Funct. Genet. 23 1995 580 587
    • (1995) Proteins: Struct. Funct. Genet. , vol.23 , pp. 580-587
    • Janin, J.1    Rodier, F.2
  • 20
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • J. Janin Specific versus non-specific contacts in protein crystals Nature Struct. Biol. 4 1997 973 974
    • (1997) Nature Struct. Biol. , vol.4 , pp. 973-974
    • Janin, J.1
  • 21
    • 0033635157 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma
    • M.E. Pacold, S. Suire, O. Perisic, S. Lara-Gonzalez, C.T. Davis, and E.H. Walker Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma Cell 103 2000 931 943
    • (2000) Cell , vol.103 , pp. 931-943
    • Pacold, M.E.1    Suire, S.2    Perisic, O.3    Lara-Gonzalez, S.4    Davis, C.T.5    Walker, E.H.6
  • 22
    • 0037953767 scopus 로고    scopus 로고
    • Crystal structure determination of FtsZ from Methanococcus jannaschii
    • J. Lowe Crystal structure determination of FtsZ from Methanococcus jannaschii J. Struct. Biol. 124 1998 235 243
    • (1998) J. Struct. Biol. , vol.124 , pp. 235-243
    • Lowe, J.1
  • 23
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • M.G. Rossmann, D. Moras, and K.W. Olsen Chemical and biological evolution of nucleotide-binding protein Nature 250 1974 194 199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 24
    • 0035907236 scopus 로고    scopus 로고
    • Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide gamma-phosphate
    • J.F. Diaz, A. Kralicek, J. Mingorance, J.M. Palacios, M. Vicente, and J.M. Andreu Activation of cell division protein FtsZ. Control of switch loop T3 conformation by the nucleotide gamma-phosphate J. Biol. Chem. 276 2001 17307 17315
    • (2001) J. Biol. Chem. , vol.276 , pp. 17307-17315
    • Diaz, J.F.1    Kralicek, A.2    Mingorance, J.3    Palacios, J.M.4    Vicente, M.5    Andreu, J.M.6
  • 25
    • 19044391883 scopus 로고    scopus 로고
    • Site-specific mutations of FtsZ - Effects on GTPase and in vitro assembly
    • C. Lu, J. Stricker, and H.P. Erickson Site-specific mutations of FtsZ - effects on GTPase and in vitro assembly BMC Microbiol. 1 2001 7
    • (2001) BMC Microbiol. , vol.1 , pp. 7
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 26
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
    • D.J. Scheffers, J.G. de Wit, T. den Blaauwen, and A.J. Driessen GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers Biochemistry 41 2002 521 529
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.J.1    De Wit, J.G.2    Den Blaauwen, T.3    Driessen, A.J.4
  • 27
    • 0043062671 scopus 로고    scopus 로고
    • In vivo characterization of Escherichia coli ftsZ mutants: Effects on Z-ring structure and function
    • J. Stricker, and H.P. Erickson In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function J. Bacteriol. 185 2003 4796 4805
    • (2003) J. Bacteriol. , vol.185 , pp. 4796-4805
    • Stricker, J.1    Erickson, H.P.2
  • 28
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • J. Goldberg Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching Cell 95 1998 237 248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 29
    • 0030589139 scopus 로고    scopus 로고
    • Structure of the GDP-Pi complex of Gly203-→Ala gialpha1: A mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis
    • A.M. Berghuis, E. Lee, A.S. Raw, A.G. Gilman, and S.R. Sprang Structure of the GDP-Pi complex of Gly203-→Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis Structure 4 1996 1277 1290
    • (1996) Structure , vol.4 , pp. 1277-1290
    • Berghuis, A.M.1    Lee, E.2    Raw, A.S.3    Gilman, A.G.4    Sprang, S.R.5
  • 30
    • 0029113233 scopus 로고
    • The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
    • S.E. Greasley, H. Jhoti, C. Teahan, R. Solari, A. Fensome, and G.M. Thomas The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms Nature Struct. Biol. 2 1995 797 806
    • (1995) Nature Struct. Biol. , vol.2 , pp. 797-806
    • Greasley, S.E.1    Jhoti, H.2    Teahan, C.3    Solari, R.4    Fensome, A.5    Thomas, G.M.6
  • 32
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 a resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
    • L.A. Tong, A.M. de Vos, M.V. Milburn, and S.H. Kim Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP J. Mol. Biol. 217 1991 503 516
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-516
    • Tong, L.A.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.H.4
  • 33
    • 0034483903 scopus 로고    scopus 로고
    • Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: The structural basis for catalysis
    • A. Heroux, E.L. White, L.J. Ross, A.P. Kuzin, and D.W. Borhani Substrate deformation in a hypoxanthine-guanine phosphoribosyltransferase ternary complex: the structural basis for catalysis Struct. Fold. Des. 8 2000 1309 1318
    • (2000) Struct. Fold. Des. , vol.8 , pp. 1309-1318
    • Heroux, A.1    White, E.L.2    Ross, L.J.3    Kuzin, A.P.4    Borhani, D.W.5
  • 34
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • S.R. Sprang G protein mechanisms: insights from structural analysis Annu. Rev. Biochem. 66 1997 639 678
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 35
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • I.R. Vetter, and A. Wittinghofer The guanine nucleotide-binding switch in three dimensions Science 294 2001 1299 1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 36
    • 0027965652 scopus 로고
    • Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis
    • D.E. Coleman, A.M. Berghuis, E. Lee, M.E. Linder, A.G. Gilman, and S.R. Sprang Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis Science 265 1994 1405 1412
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 37
    • 0039374565 scopus 로고    scopus 로고
    • Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ
    • T.M. Sossong Jr, M.R. Brigham-Burke, P. Hensley, and K.H. Pearce Jr Self-activation of guanosine triphosphatase activity by oligomerization of the bacterial cell division protein FtsZ Biochemistry 38 1999 14843 14850
    • (1999) Biochemistry , vol.38 , pp. 14843-14850
    • Sossong Jr., T.M.1    Brigham-Burke, M.R.2    Hensley, P.3    Pearce Jr., K.H.4
  • 38
    • 0042357108 scopus 로고    scopus 로고
    • Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments
    • M.A. Oliva, S. Huecas, J.M. Palacios, J. Martin-Benito, J.M. Valpuesta, and J.M. Andreu Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments J. Biol. Chem. 278 2003 33562 33570
    • (2003) J. Biol. Chem. , vol.278 , pp. 33562-33570
    • Oliva, M.A.1    Huecas, S.2    Palacios, J.M.3    Martin-Benito, J.4    Valpuesta, J.M.5    Andreu, J.M.6
  • 39
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • S.T. Cole, R. Brosch, J. Parkhill, T. Garnier, C. Churcher, and D. Harris Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence Nature 393 1998 537 544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N
    • Collaborative Computational Project, N The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 44
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallog. sect. A 50 1994 157 163
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjelgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 48
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A.A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallog. 30 1997 1022 1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 49
    • 0000449646 scopus 로고
    • Improvement of macro-molecular electron-density maps by the simultaneous application of real and reciprocal space constraints
    • K.D. Cowtan, and P. Main Improvement of macro-molecular electron-density maps by the simultaneous application of real and reciprocal space constraints Acta Crystallog. sect. D 49 1993 148 157
    • (1993) Acta Crystallog. Sect. D , vol.49 , pp. 148-157
    • Cowtan, K.D.1    Main, P.2
  • 50
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 51
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 53
    • 0025398721 scopus 로고
    • WHATIF: A molecular modelling and drug design program
    • G. Vriend WHATIF: a molecular modelling and drug design program J. Mol. Graph. 8 1990 52 56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.