메뉴 건너뛰기




Volumn 16, Issue 10, 2009, Pages 1068-1073

High-resolution structure of the rotor ring of a proton-dependent ATP synthase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); CATION; GLUTAMIC ACID; HYDRONIUM ION; MEMBRANE LIPID; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 70349828967     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1678     Document Type: Article
Times cited : (166)

References (49)
  • 1
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase-some probabilities and possibilities
    • Boyer, P.D. The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 2
    • 0028114231 scopus 로고
    • 1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G.W., Lutter, R. & Walker, J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628 (1994).
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 4
    • 66249132322 scopus 로고    scopus 로고
    • 1 -ATPase
    • Junge, W., Sielaff, H. & Engelbrecht, S. Torque generation and elastic power transmission in the rotary FoF1-ATPase. Nature 459, 364-370 (2009).
    • (2009) Nature , vol.459 , pp. 364-370
    • Junge, W.1    Sielaff, H.2    Engelbrecht, S.3
  • 5
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A.G.W. & Walker, J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705 (1999).
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 6
    • 27644566520 scopus 로고    scopus 로고
    • o symmetry mismatch is not obligatory
    • Pogoryelov, D. et al. The c15 ring of the Spirulina platensis F-ATP synthase: F1/Fo symmetry mismatch is not obligatory. EMBO Rep. 6, 1040-1044 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 1040-1044
    • Pogoryelov, D.1
  • 7
    • 17844367330 scopus 로고    scopus 로고
    • +-ATPase from Ilyobacter tartaricus
    • Meier, T., Polzer, P. , Diederichs, K., Welte, W. & Dimroth, P. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science 308, 659-662 (2005).
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 8
    • 67650684937 scopus 로고    scopus 로고
    • +-dependent F-ATP synthases
    • Meier, T. et al. Complete ion-coordination structure in the rotor ring of Na+-dependent F-ATP synthases. J. Mol. Biol. 391, 498-507 (2009).
    • (2009) J. Mol. Biol. , vol.391 , pp. 498-507
    • Meier, T.1
  • 9
    • 0023658657 scopus 로고
    • 1 -ATPase: A requirement for arginine at position 210 of the a-subunit
    • Lightowlers, R.N., Howitt, S.M., Hatch, L., Gibson, F. & Cox, G.B. The proton pore in the Escherichia coli FoF1-ATPase: a requirement for arginine at position 210 of the a-subunit. Biochim. Biophys. Acta 894, 399-406 (1987).
    • (1987) Biochim. Biophys. Acta , vol.894 , pp. 399-406
    • Lightowlers, R.N.1    Howitt, S.M.2    Hatch, L.3    Gibson, F.4    Cox, G.B.5
  • 10
    • 0024977998 scopus 로고
    • o ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • Cain, B.D. & Simoni, R.D. Proton translocation by the F1FoATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264, 3292-3300 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 11
    • 0026099432 scopus 로고
    • 1) a subunit from Escherichia coli
    • Eya, S., Maeda, M. & Futai, M. Role of the carboxyl terminal region of H+-ATPase (FoF1) a subunit from Escherichia coli. Arch. Biochem. Biophys. 284, 71-77 (1991).
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 71-77
    • Eya, S.1    Maeda, M.2    Futai, M.3
  • 12
    • 33745882947 scopus 로고    scopus 로고
    • o -ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum
    • Ferguson, S.A., Keis, S. & Cook, G.M. Biochemical and molecular characterization of a Na+-translocating F1Fo-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum. J. Bacteriol. 188, 5045-5054 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 5045-5054
    • Ferguson, S.A.1    Keis, S.2    Cook, G.M.3
  • 13
    • 0023656441 scopus 로고
    • o type
    • Laubinger, W. & Dimroth, P. Characterization of the Na+-stimulated ATPase of Propionigenium modestum as an enzyme of the F1Fo type. Eur. J. Biochem. 168, 475-480 (1987).
    • (1987) Eur. J. Biochem. , vol.168 , pp. 475-480
    • Laubinger, W.1    Dimroth, P.2
  • 14
    • 0031595839 scopus 로고    scopus 로고
    • o ATPase of Ilyobacter tartaricus, a sodium ion pump
    • Neumann, S., Matthey, U., Kaim, G. & Dimroth, P. Purifcation and properties of the F1Fo ATPase of Ilyobacter tartaricus, a sodium ion pump. J. Bacteriol. 180, 3312-3316 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 3312-3316
    • Neumann, S.1    Matthey, U.2    Kaim, G.3    Dimroth, P.4
  • 15
    • 0028224825 scopus 로고
    • o-type enzyme
    • Reidlinger, J. & Müller, V. Purifcation of ATP synthase from Acetobacterium woodii and identifcation as a Na+-translocating F1Fo-type enzyme. Eur. J. Biochem. 223, 275-283 (1994).
    • (1994) Eur. J. Biochem. , vol.223 , pp. 275-283
    • Reidlinger, J.1    Müller, V.2
  • 16
    • 67650546998 scopus 로고    scopus 로고
    • 14 rotor ring of the proton translocating chloroplast ATP synthase
    • Vollmar, M., Schlieper, D., Winn, M., Büchner, C. & Groth, G. Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase. J. Biol. Chem. 284, 18228-18235 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 18228-18235
    • Vollmar, M.1    Schlieper, D.2    Winn, M.3    Büchner, C.4    Groth, G.5
  • 18
    • 0027180769 scopus 로고
    • + -ATP synthase and unusual thermodynamic properties in the alkalophilic cyanobacterium Spirulina platensis
    • Bakels, R.H., van Walraven, H.S., Krab, K., Scholts, M.J. & Kraayenhof, R. On the activation mechanism of the H+-ATP synthase and unusual thermodynamic properties in the alkalophilic cyanobacterium Spirulina platensis. Eur. J. Biochem. 213, 957-964 (1993).
    • (1993) Eur. J. Biochem. , vol.213 , pp. 957-964
    • Bakels, R.H.1    Van Walraven, H.S.2    Krab, K.3    Scholts, M.J.4    Kraayenhof, R.5
  • 19
    • 49149117541 scopus 로고    scopus 로고
    • 14 -rotor of the chloroplast ATP synthase reveals that it contains pigments
    • Varco-Merth, B., Fromme, R., Wang, M. & Fromme, P. Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments. Biochim. Biophys. Acta 1777, 605-612 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 605-612
    • Varco-Merth, B.1    Fromme, R.2    Wang, M.3    Fromme, P.4
  • 20
    • 51749114028 scopus 로고    scopus 로고
    • Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus
    • Pogoryelov, D. et al. Probing the rotor subunit interface of the ATP synthase from Ilyobacter tartaricus. FEBS J. 275, 4850-4862 (2008).
    • (2008) FEBS J. , vol.275 , pp. 4850-4862
    • Pogoryelov, D.1
  • 22
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the γ-ε Complex of ATP synthase
    • Rodgers, A.J. & Wilce, M.C. Structure of the γ-ε complex of ATP synthase. Nat. Struct. Biol. 7, 1051-1054 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.1    Wilce, M.C.2
  • 23
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride
    • Guskov, A. et al. Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 16, 334-342 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 334-342
    • Guskov, A.1
  • 24
    • 0036386340 scopus 로고    scopus 로고
    • +-ATP synthase
    • Vonck, J. et al. Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase. J. Mol. Biol. 321, 307-316 (2002).
    • (2002) J. Mol. Biol. , vol.321 , pp. 307-316
    • Vonck, J.1
  • 25
    • 0035929328 scopus 로고    scopus 로고
    • The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids
    • Meier, T., Matthey, U., Henzen, F., Dimroth, P. & Müller, D.J. The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids. FEBS Lett. 505, 353-356 (2001).
    • (2001) FEBS Lett. , vol.505 , pp. 353-356
    • Meier, T.1    Matthey, U.2    Henzen, F.3    Dimroth, P.4    Müller, D.J.5
  • 26
    • 17844369968 scopus 로고    scopus 로고
    • +-ATPase from Enterococcus hirae
    • DOI 10.1126/science.1110064
    • Murata, T., Yamato, I., Kakinuma, Y., Leslie, A.G. & Walker, J.E. Structure of the rotor of the V-type Na+-ATPase from Enterococcus hirae. Science 308, 654-659 (2005). (Pubitemid 40594379)
    • (2005) Science , vol.308 , Issue.5722 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.W.4    Walker, J.E.5
  • 27
    • 0037227431 scopus 로고    scopus 로고
    • Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases
    • Meier, T. et al. Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases. J. Mol. Biol. 325, 389-397 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 389-397
    • Meier, T.1
  • 28
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation?
    • Boyer, P.D. Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation? Trends Biochem. Sci. 13, 5-7 (1988).
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 5-7
    • Boyer, P.D.1
  • 29
    • 35448959682 scopus 로고    scopus 로고
    • Two distinct proton binding sites in the ATP synthase family
    • von Ballmoos, C. & Dimroth, P. Two distinct proton binding sites in the ATP synthase family. Biochemistry 46, 11800-11809 (2007).
    • (2007) Biochemistry , vol.46 , pp. 11800-11809
    • Von Ballmoos, C.1    Dimroth, P.2
  • 30
    • 66149118618 scopus 로고    scopus 로고
    • + -ATP synthase from chloroplasts
    • Chen, M.F., Wang, J.D. & Su, T.M. Concentration gradient effects of sodium and lithium ions and deuterium isotope effects on the activities of H+-ATP synthase from chloroplasts. Biophys. J. 96, 2479-2489 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 2479-2489
    • Chen, M.F.1    Wang, J.D.2    Su, T.M.3
  • 31
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • Kaim, G., Wehrle, F. , Gerike, U. & Dimroth, P. Molecular basis for the coupling ion selectivity of F1Fo ATP synthases: probing the liganding groups for Na+ and Li+ in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36, 9185-9194 (1997).
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 32
    • 38349109850 scopus 로고    scopus 로고
    • Alternative proton binding mode in ATP synthases
    • von Ballmoos, C. Alternative proton binding mode in ATP synthases. J. Bioenerg. Biomembr. 39, 441-445 (2007).
    • (2007) J. Bioenerg. Biomembr. , vol.39 , pp. 441-445
    • Von Ballmoos, C.1
  • 34
    • 0345599038 scopus 로고    scopus 로고
    • Sodium dependency of the photosynthetic electron transport in the alkaliphilic cyanobacterium Arthrospira platensis
    • Pogoryelov, D. et al. Sodium dependency of the photosynthetic electron transport in the alkaliphilic cyanobacterium Arthrospira platensis. J. Bioenerg. Biomembr. 35, 427-437 (2003).
    • (2003) J. Bioenerg. Biomembr. , vol.35 , pp. 427-437
    • Pogoryelov, D.1
  • 35
    • 0031464314 scopus 로고    scopus 로고
    • 1-ATP synthase
    • Valiyaveetil, F.I. & Fillingame, R.H. On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli FoF1-ATP synthase. J. Biol. Chem. 272, 32635-32641 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 32635-32641
    • Valiyaveetil, F.I.1    Fillingame, R.H.2
  • 36
    • 0036383051 scopus 로고    scopus 로고
    • o motor probed by mutational analyses of subunit a
    • Wehrle, F. , Kaim, G. & Dimroth, P. Molecular mechanism of the ATP synthase s Fo motor probed by mutational analyses of subunit a. J. Mol. Biol. 322, 369-381 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 369-381
    • Wehrle, F.1    Kaim, G.2    Dimroth, P.3
  • 37
    • 45549098592 scopus 로고    scopus 로고
    • o ATP synthase
    • Steed, P.R. & Fillingame, R.H. Subunit a facilitates aqueous access to a membrane-embedded region of subunit c in Escherichia coli F1Fo ATP synthase. J. Biol. Chem. 283, 12365-12372 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 12365-12372
    • Steed, P.R.1    Fillingame, R.H.2
  • 38
    • 2942675081 scopus 로고    scopus 로고
    • The of ATP synthase: Ohmic conductance (10 fS), and absence of voltage gating
    • Feniouk, B.A. et al. The of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating. Biophys. J. 86, 4094-4109 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 4094-4109
    • Feniouk, B.A.1
  • 39
    • 57649119786 scopus 로고    scopus 로고
    • Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase
    • Moore, K.J. & Fillingame, R.H. Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. J. Biol. Chem. 283, 31726-31735 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31726-31735
    • Moore, K.J.1    Fillingame, R.H.2
  • 40
    • 69949161477 scopus 로고    scopus 로고
    • o ATP synthase
    • Steed, P.R. & Fillingame, R.H. Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1Fo ATP synthase. J. Biol. Chem. 284, 23243-23250 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 23243-23250
    • Steed, P.R.1    Fillingame, R.H.2
  • 41
    • 0036479141 scopus 로고    scopus 로고
    • o ATP synthase
    • von Ballmoos, C. et al. Membrane topography of the coupling ion binding site in Na+-translocating F1Fo ATP synthase. J. Biol. Chem. 277, 3504-3510 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3504-3510
    • Von Ballmoos, C.1
  • 42
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • Fillingame, R.H., Angevine, C.M. & Dmitriev, O.Y. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 555, 29-34 (2003).
    • (2003) FEBS Lett. , vol.555 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 43
    • 3242781685 scopus 로고    scopus 로고
    • + -translocating activity together with subunits a and c
    • Greie, J.C., Heitkamp, T. & Altendorf, K. The transmembrane domain of subunit b of the Escherichia coli F1Fo ATP synthase is suffcient for H+-translocating activity together with subunits a and c. Eur. J. Biochem. 271, 3036-3042 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3036-3042
    • Greie, J.C.1    Heitkamp, T.2    Altendorf, K.3
  • 44
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs, K. & Karplus, P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 45
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 46
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 47
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modifcation and model building
    • Terwilliger, T. SOLVE and RESOLVE: automated structure solution, density modifcation and model building. J. Synchrotron Radiat. 11, 49-52 (2004).
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 49-52
    • Terwilliger, T.1
  • 49
    • 49649085631 scopus 로고    scopus 로고
    • Automated structure solution with the PHENIX suite
    • Zwart, P.H. et al. Automated structure solution with the PHENIX suite. Methods Mol. Biol. 426, 419-435 (2008).
    • (2008) Methods Mol. Biol. , vol.426 , pp. 419-435
    • Zwart, P.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.