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Volumn 366, Issue 3, 2007, Pages 933-944

Dimeric Core Structure of Modular Stator Subunit E of Archaeal H+-ATPase

Author keywords

A ATPase; crystal structure; stator; subunit E; V ATPase

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 33846625950     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.088     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106 (2001) 331-341
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3
  • 7
    • 0031445914 scopus 로고    scopus 로고
    • Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis
    • Boekema E.J., Ubbink-Kok T., Lolkema J.S., Brisson A., and Konings W.N. Visualization of a peripheral stalk in V-type ATPase: evidence for the stator structure essential to rotational catalysis. Proc. Natl Acad. Sci. USA 94 (1997) 14291-14293
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14291-14293
    • Boekema, E.J.1    Ubbink-Kok, T.2    Lolkema, J.S.3    Brisson, A.4    Konings, W.N.5
  • 8
    • 0033527743 scopus 로고    scopus 로고
    • Structure of the vacuolar ATPase by electron microscopy
    • Wilkens S., Vasilyeva E., and Forgac M. Structure of the vacuolar ATPase by electron microscopy. J. Biol. Chem. 274 (1999) 31804-31810
    • (1999) J. Biol. Chem. , vol.274 , pp. 31804-31810
    • Wilkens, S.1    Vasilyeva, E.2    Forgac, M.3
  • 9
    • 0023930674 scopus 로고
    • Topography and subunit stoichiometry of the coated vesicle proton pump
    • Arai H., Terres G., Pink S., and Forgac M. Topography and subunit stoichiometry of the coated vesicle proton pump. J. Biol. Chem. 263 (1988) 8796-8802
    • (1988) J. Biol. Chem. , vol.263 , pp. 8796-8802
    • Arai, H.1    Terres, G.2    Pink, S.3    Forgac, M.4
  • 11
    • 0037125922 scopus 로고    scopus 로고
    • Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B
    • Arata Y., Baleja J.D., and Forgac M. Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B. Biochemistry 41 (2002) 11301-11307
    • (2002) Biochemistry , vol.41 , pp. 11301-11307
    • Arata, Y.1    Baleja, J.D.2    Forgac, M.3
  • 12
    • 33646541995 scopus 로고    scopus 로고
    • Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk
    • Maegawa Y., Morita H., Iyaguchi D., Yao M., Watanabe N., and Tanaka I. Structure of the catalytic nucleotide-binding subunit A of A-type ATP synthase from Pyrococcus horikoshii reveals a novel domain related to the peripheral stalk. Acta Crystallog. sect. D 62 (2006) 483-488
    • (2006) Acta Crystallog. sect. D , vol.62 , pp. 483-488
    • Maegawa, Y.1    Morita, H.2    Iyaguchi, D.3    Yao, M.4    Watanabe, N.5    Tanaka, I.6
  • 13
    • 33646028171 scopus 로고    scopus 로고
    • Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Go1: implications of nucleotide-binding differences in the major A1Ao subunits A and B
    • Schäfer I.B., Bailer S.M., Düser M.G., Börsch M., Bernal R.A., Stock D., and Grüber G. Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Go1: implications of nucleotide-binding differences in the major A1Ao subunits A and B. J. Mol. Biol. 358 (2006) 725-740
    • (2006) J. Mol. Biol. , vol.358 , pp. 725-740
    • Schäfer, I.B.1    Bailer, S.M.2    Düser, M.G.3    Börsch, M.4    Bernal, R.A.5    Stock, D.6    Grüber, G.7
  • 14
    • 0027169669 scopus 로고
    • Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme
    • Doherty R.D., and Kane P.M. Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme. J. Biol. Chem. 268 (1993) 16845-16851
    • (1993) J. Biol. Chem. , vol.268 , pp. 16845-16851
    • Doherty, R.D.1    Kane, P.M.2
  • 15
    • 0344875467 scopus 로고    scopus 로고
    • 1-ATPase: affinity purification and structural features by electron microscopy
    • 1-ATPase: affinity purification and structural features by electron microscopy. J. Biol. Chem. 278 (2003) 47299-47306
    • (2003) J. Biol. Chem. , vol.278 , pp. 47299-47306
    • Zhang, Z.1    Charsky, C.2    Kane, P.M.3    Wilkens, S.4
  • 16
    • 0142089024 scopus 로고    scopus 로고
    • Assembly and regulation of the yeast vacuolar H+-ATPase
    • Kane P.M., and Smardon A.M. Assembly and regulation of the yeast vacuolar H+-ATPase. J. Bioenerg. Biomembr. 35 (2003) 313-321
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 313-321
    • Kane, P.M.1    Smardon, A.M.2
  • 19
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 20
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the sterochemical quality of protein structures
    • Laskowski R.A., Macarthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the sterochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 21
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L., and Sander C. Touring protein fold space with Dali/FSSP. Nucl. Acids Res. 26 (1998) 316-319
    • (1998) Nucl. Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 22
    • 0029643858 scopus 로고    scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations
    • Bujacz G., Jaskolski M., Alexandratos J., Wlodawer A., Merkel G., Katz R.A., and Skalka A.M. The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure 4 (1996) 89-96
    • (1996) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 23
    • 0031297461 scopus 로고    scopus 로고
    • Specific versus non-specific contacts in protein crystals
    • Janin J. 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
  • 24
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 28
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • Rubinstein J.L., Walker J.E., and Henderson R. Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J. 22 (2003) 6182-6192
    • (2003) EMBO J. , vol.22 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 29
    • 0037188394 scopus 로고    scopus 로고
    • The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain
    • Del Rizzo P.A., Bi Y., Dunn S.D., and Shilton B.H. The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry 41 (2002) 6875-6884
    • (2002) Biochemistry , vol.41 , pp. 6875-6884
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3    Shilton, B.H.4
  • 31
    • 4644354650 scopus 로고    scopus 로고
    • Building the stator of the yeast vacuolar-ATPase: specific interaction between subunits E and G
    • Féthière J., Venzke D., Diepholz M., Seybert A., Geerlof A., Gentzel M., et al. Building the stator of the yeast vacuolar-ATPase: specific interaction between subunits E and G. J. Biol. Chem. 279 (2004) 40670-40676
    • (2004) J. Biol. Chem. , vol.279 , pp. 40670-40676
    • Féthière, J.1    Venzke, D.2    Diepholz, M.3    Seybert, A.4    Geerlof, A.5    Gentzel, M.6
  • 32
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • Shao E., and Forgac M. Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J. Biol. Chem. 279 (2004) 48663-48670
    • (2004) J. Biol. Chem. , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 33
    • 4644343538 scopus 로고    scopus 로고
    • Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy
    • Coskun U., Chaban Y.L., Lingl A., Müller V., Keegstra W., Boekema E.J., and Grüber G. Structure and subunit arrangement of the A-type ATP synthase complex from the archaeon Methanococcus jannaschii visualized by electron microscopy. J. Biol. Chem. 279 (2004) 38644-38648
    • (2004) J. Biol. Chem. , vol.279 , pp. 38644-38648
    • Coskun, U.1    Chaban, Y.L.2    Lingl, A.3    Müller, V.4    Keegstra, W.5    Boekema, E.J.6    Grüber, G.7
  • 34
    • 33646470459 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary crystallographic analysis of the vacuole-type ATPase subunit E from Pyrococcus horikoshii OT3
    • Lokanath N.K., Ukita Y., Sugahara M., and Kunishima N. Purification, crystallization and preliminary crystallographic analysis of the vacuole-type ATPase subunit E from Pyrococcus horikoshii OT3. Acta Crystallog. sect. F 61 (2005) 56-58
    • (2005) Acta Crystallog. sect. F , vol.61 , pp. 56-58
    • Lokanath, N.K.1    Ukita, Y.2    Sugahara, M.3    Kunishima, N.4
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. 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
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0035210945 scopus 로고    scopus 로고
    • Maximum-likelihood density modification with pattern recognition of structural motifs
    • Terwilliger T.C. Maximum-likelihood density modification with pattern recognition of structural motifs. Acta Crystallog. sect. D 57 (2001) 1755-1762
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1755-1762
    • Terwilliger, T.C.1
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project No. 4. 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
  • 41
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Venyaminov S.Y., and Woody R.W. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8 (1999) 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 42
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24 (1991) 946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 43
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to Molscript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to Molscript version 1.4, including reading and contouring of electron-density maps. Acta Crystallog. sect. D 55 (1999) 938-940
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 44
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: photorealistic molecular graphics
    • Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 (1997) 505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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