메뉴 건너뛰기




Volumn 1777, Issue 2, 2008, Pages 227-237

Interaction of transmembrane helices in ATP synthase subunit a in solution as revealed by spin label difference NMR

Author keywords

ATP synthase subunit a; Membrane protein structure; Proton transport; Solution NMR; Spin label; Transmembrane helices

Indexed keywords

CHLOROFORM; METHANOL; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SOLVENT;

EID: 38549122201     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.11.011     Document Type: Article
Times cited : (8)

References (52)
  • 3
    • 33645796449 scopus 로고    scopus 로고
    • Catalytic and mechanical cycles in F-ATP synthases
    • Dimroth P., von Ballmoos C., and Meier T. Catalytic and mechanical cycles in F-ATP synthases. EMBO Rep. 7 (2006) 276-282
    • (2006) EMBO Rep. , vol.7 , pp. 276-282
    • Dimroth, P.1    von Ballmoos, C.2    Meier, T.3
  • 4
    • 0023839098 scopus 로고
    • ATP synthesis by oxidative phosphorylation
    • Senior A.E. ATP synthesis by oxidative phosphorylation. Physiol. Rev. 68 (1988) 177-231
    • (1988) Physiol. Rev. , vol.68 , pp. 177-231
    • Senior, A.E.1
  • 5
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is ten
    • Jiang W., Hermolin J., and Fillingame R.H. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is ten. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 4966-4971
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 8
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 11
    • 0033529291 scopus 로고    scopus 로고
    • o ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme
    • o ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7785-7790
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7785-7790
    • Dmitriev, O.Y.1    Jones, P.C.2    Fillingame, R.H.3
  • 13
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V.K., and Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402 (1999) 263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 16
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • Angevine C.M., and Fillingame R.H. Aqueous access channels in subunit a of rotary ATP synthase. J. Biol. Chem. 278 (2003) 6066-6074
    • (2003) J. Biol. Chem. , vol.278 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 17
    • 0345255628 scopus 로고    scopus 로고
    • Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane
    • Angevine C.M., Herold K.A., and Fillingame R.H. Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13179-13183
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13179-13183
    • Angevine, C.M.1    Herold, K.A.2    Fillingame, R.H.3
  • 18
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5
    • Angevine C.M., Herold K.A., Vincent O.D., and Fillingame R.H. Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5. J. Biol. Chem. 282 (2007) 9001-9007
    • (2007) J. Biol. Chem. , vol.282 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.2    Vincent, O.D.3    Fillingame, R.H.4
  • 20
    • 0032568845 scopus 로고    scopus 로고
    • o ATP synthase as determined by labeling of unique cysteine residues
    • o ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273 (1998) 16235-16240
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 21
    • 0033546193 scopus 로고    scopus 로고
    • A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase
    • Wada T., Long J.C., Zhang D., and Vik S.B. A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J. Biol. Chem. 274 (1999) 17353-17357
    • (1999) J. Biol. Chem. , vol.274 , pp. 17353-17357
    • Wada, T.1    Long, J.C.2    Zhang, D.3    Vik, S.B.4
  • 22
    • 0032499690 scopus 로고    scopus 로고
    • o ATP synthase of Escherichia coli defined by disulfide cross-linking
    • o ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6607-6612
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6607-6612
    • Jiang, W.1    Fillingame, R.H.2
  • 23
    • 0028880405 scopus 로고
    • The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity
    • Hatch L.P., Cox G.B., and Howitt S.M. The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J. Biol. Chem. 270 (1995) 29407-29412
    • (1995) J. Biol. Chem. , vol.270 , pp. 29407-29412
    • Hatch, L.P.1    Cox, G.B.2    Howitt, S.M.3
  • 26
    • 0034613389 scopus 로고    scopus 로고
    • 1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme
    • 1 ATP synthase from the cross-linking of subunits b and c in the Escherichia coli enzyme. J. Biol. Chem. 275 (2000) 31340-31346
    • (2000) J. Biol. Chem. , vol.275 , pp. 31340-31346
    • Jones, P.C.1    Hermolin, J.2    Jiang, W.3    Fillingame, R.H.4
  • 27
    • 0033960457 scopus 로고    scopus 로고
    • Coupling H[+] transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor
    • Fillingame R.H., Jiang W., and Dmitriev O.Y. Coupling H[+] transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor. J. Exp. Biol. 203 (2000) 9-17
    • (2000) J. Exp. Biol. , vol.203 , pp. 9-17
    • Fillingame, R.H.1    Jiang, W.2    Dmitriev, O.Y.3
  • 28
    • 0028560446 scopus 로고
    • o ATP synthase in Escherichia coli
    • o ATP synthase in Escherichia coli. J. Biol. Chem. 269 (1994) 32313-32317
    • (1994) J. Biol. Chem. , vol.269 , pp. 32313-32317
    • Hartzog, P.E.1    Cain, B.D.2
  • 29
    • 33845989502 scopus 로고    scopus 로고
    • Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle
    • Schwem B.E., and Fillingame R.H. Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. J. Biol. Chem. 49 (2006) 37861-37867
    • (2006) J. Biol. Chem. , vol.49 , pp. 37861-37867
    • Schwem, B.E.1    Fillingame, R.H.2
  • 30
    • 0242657369 scopus 로고    scopus 로고
    • Mechanics of coupling proton movements to c-ring rotation in ATP synthase
    • Fillingame R.H., Angevine C.M., and Dmitriev O.Y. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 555 (2003) 29-34
    • (2003) FEBS Lett. , vol.555 , pp. 29-34
    • Fillingame, R.H.1    Angevine, C.M.2    Dmitriev, O.Y.3
  • 31
    • 0347985776 scopus 로고    scopus 로고
    • Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent
    • Dmitriev O.Y., Altendorf K., and Fillingame R.H. Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. FEBS Lett. 556 (2004) 35-38
    • (2004) FEBS Lett. , vol.556 , pp. 35-38
    • Dmitriev, O.Y.1    Altendorf, K.2    Fillingame, R.H.3
  • 33
    • 0034737966 scopus 로고    scopus 로고
    • A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation
    • Vik S.B., Long J.C., Wada T., and Zhang D. A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. Biochim. Biophys. Acta 1458 (2000) 457-466
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 457-466
    • Vik, S.B.1    Long, J.C.2    Wada, T.3    Zhang, D.4
  • 35
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen P.A. Spin labeling of proteins. Methods Enzymol. 177 (1989) 86-121
    • (1989) Methods Enzymol. , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 36
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • Battiste J.L., and Wagner G. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. Biochemistry 39 (2000) 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 37
    • 0025925183 scopus 로고
    • Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H[+]-ATPase
    • Iwamoto A., Omote H., Hanada H., Tomioka N., Itai A., Maeda M., and Futai M. Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H[+]-ATPase. J. Biol. Chem. 266 (1991) 16350-16355
    • (1991) J. Biol. Chem. , vol.266 , pp. 16350-16355
    • Iwamoto, A.1    Omote, H.2    Hanada, H.3    Tomioka, N.4    Itai, A.5    Maeda, M.6    Futai, M.7
  • 39
    • 0029682322 scopus 로고    scopus 로고
    • Site-directed mutagenesis in vitro by megaprimer PCR
    • Barik S. Site-directed mutagenesis in vitro by megaprimer PCR. Methods Mol. Biol. 57 (1996) 203-215
    • (1996) Methods Mol. Biol. , vol.57 , pp. 203-215
    • Barik, S.1
  • 41
    • 0021756359 scopus 로고
    • The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase
    • Walker J.E., Saraste J.E., and Gay N.J. The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase. Biochim. Biophys. Acta 768 (1984) 164-200
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, J.E.2    Gay, N.J.3
  • 42
    • 0022554096 scopus 로고
    • Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase
    • Penefsky H.S. Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase. Methods Enzymol. 126 (1986) 608-618
    • (1986) Methods Enzymol. , vol.126 , pp. 608-618
    • Penefsky, H.S.1
  • 43
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K., Riek R., Wider G., and Wüthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 12366-12371
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 44
    • 0033599567 scopus 로고    scopus 로고
    • TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein
    • Yang D., and Kay L.E. TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein. J. Am. Chem. Soc. 121 (1999) 2571-2575
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2571-2575
    • Yang, D.1    Kay, L.E.2
  • 46
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delagio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delagio, F.2    Bax, A.3
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 48
    • 0034909370 scopus 로고    scopus 로고
    • Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin
    • Katragadda M., Alderfer J.L., and Yeagle P.L. Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Biophys. J. 81 (2001) 1029-1036
    • (2001) Biophys. J. , vol.81 , pp. 1029-1036
    • Katragadda, M.1    Alderfer, J.L.2    Yeagle, P.L.3
  • 50
    • 20544431791 scopus 로고    scopus 로고
    • Structure and dynamics of the second and third transmembrane domains of human glycine receptor
    • Ma D., Liu Z., Li L., Tang P., and Xu Y. Structure and dynamics of the second and third transmembrane domains of human glycine receptor. Biochemistry 44 (2005) 8790-8800
    • (2005) Biochemistry , vol.44 , pp. 8790-8800
    • Ma, D.1    Liu, Z.2    Li, L.3    Tang, P.4    Xu, Y.5
  • 51
    • 34250873336 scopus 로고    scopus 로고
    • Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin
    • Wehbi H., Rath A., Glibowicka M., and Deber C.M. Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin. Biochemistry 46 (2007) 7099-7106
    • (2007) Biochemistry , vol.46 , pp. 7099-7106
    • Wehbi, H.1    Rath, A.2    Glibowicka, M.3    Deber, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.