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Volumn 40, Issue 3, 2008, Pages 157-163

GFT projection NMR based resonance assignment of membrane proteins: Application to subunit c of E. coli F1F0 ATP synthase in LPPG micelles

Author keywords

F1F0ATP synthase; GFT NMR; LPPG; Membrane protein; Projection NMR; Resonance assignment; Subunitc

Indexed keywords

LYSOPALMITOYLPHOSPHATIDYLGLYCEROL; MEMBRANE PROTEIN; PHOSPHATIDYLGLYCEROL; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 41149103328     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9224-8     Document Type: Article
Times cited : (16)

References (38)
  • 1
    • 3042788977 scopus 로고    scopus 로고
    • G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment
    • Atreya HS, Szyperski T (2004) G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment. Proc Natl Acad Sci USA 101:9642-9647
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9642-9647
    • Atreya, H.S.1    Szyperski, T.2
  • 4
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T, Billeter M, Guntert P, Wüthrich K (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 6:1-10
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Guntert, P.4    Wüthrich, K.5
  • 6
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill JH, Louis JM, Miller C, Bax A (2006) NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci 15:684-698
    • (2006) Protein Sci , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 7
    • 0035920241 scopus 로고    scopus 로고
    • Structure of Ala(20) → Pro/Pro(64) → Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices
    • Dmitriev OY, Fillingame RH (2001) Structure of Ala(20) → Pro/ Pro(64) → Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices. J Biol Chem 276:27449-27454
    • (2001) J Biol Chem , vol.276 , pp. 27449-27454
    • Dmitriev, O.Y.1    Fillingame, R.H.2
  • 8
    • 0037197659 scopus 로고    scopus 로고
    • Structure of Ala24/Asp61 → Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: Implications for the mechanism of proton transport and rotary movement in the F 0 complex
    • Dmitriev OY, Abildgaard F, Markley JL, Fillingame RH (2002) Structure of Ala24/Asp61 → Asp24/Asn61 substituted subunit c of Escherichia coli ATP synthase: Implications for the mechanism of proton transport and rotary movement in the F 0 complex. Biochemistry 41:5537-5547
    • (2002) Biochemistry , vol.41 , pp. 5537-5547
    • Dmitriev, O.Y.1    Abildgaard, F.2    Markley, J.L.3    Fillingame, R.H.4
  • 9
    • 24744454144 scopus 로고    scopus 로고
    • High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection
    • Eghbalnia HR, Bahrami A, Tonelli M, Hallenga K, Markley JL (2005) High-resolution iterative frequency identification for NMR as a general strategy for multidimensional data collection. J Am Chem Soc 127:12528-12536
    • (2005) J Am Chem Soc , vol.127 , pp. 12528-12536
    • Eghbalnia, H.R.1    Bahrami, A.2    Tonelli, M.3    Hallenga, K.4    Markley, J.L.5
  • 10
    • 27144465980 scopus 로고    scopus 로고
    • Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HC CH NMR spectroscopy
    • Eletsky A, Atreya HS, Liu G, Szyperski T (2005) Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HC CH NMR spectroscopy. J Am Chem Soc 127:14578-14579
    • (2005) J Am Chem Soc , vol.127 , pp. 14578-14579
    • Eletsky, A.1    Atreya, H.S.2    Liu, G.3    Szyperski, T.4
  • 12
    • 33750918707 scopus 로고    scopus 로고
    • Recent developments in membrane protein structural genomics
    • Gao FP, Cross TA (2005) Recent developments in membrane protein structural genomics. Genome Biol 6:244
    • (2005) Genome Biol , vol.6 , pp. 244
    • Gao, F.P.1    Cross, T.A.2
  • 15
    • 0000088628 scopus 로고
    • Processing of multi-dimensional NMR data with the new software PROSA
    • Güntert P, Dütsch V, Wider G, Wüthrich K (1992) Processing of multi-dimensional NMR data with the new software PROSA. J Biomol NMR 2:619-629
    • (1992) J Biomol NMR , vol.2 , pp. 619-629
    • Güntert, P.1    Dütsch, V.2    Wider, G.3    Wüthrich, K.4
  • 17
    • 0037419802 scopus 로고    scopus 로고
    • GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information
    • Kim S, Szyperski T (2003) GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information. J Am Chem Soc 125:1385-1393
    • (2003) J Am Chem Soc , vol.125 , pp. 1385-1393
    • Kim, S.1    Szyperski, T.2
  • 19
    • 2442687868 scopus 로고    scopus 로고
    • Projection-reconstruction technique for speeding up multidimensional NMR spectroscopy
    • Kupce E, Freeman R (2004) Projection-reconstruction technique for speeding up multidimensional NMR spectroscopy. J Am Chem Soc 126:6429-6440
    • (2004) J Am Chem Soc , vol.126 , pp. 6429-6440
    • Kupce, E.1    Freeman, R.2
  • 21
    • 34247893770 scopus 로고    scopus 로고
    • Structural genomics and drug discovery
    • Lundstrom K (2007) Structural genomics and drug discovery. J Cell Mol Med 11: 224-238
    • (2007) J Cell Mol Med , vol.11 , pp. 224-238
    • Lundstrom, K.1
  • 22
    • 0033560680 scopus 로고    scopus 로고
    • NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles
    • Matthey U, Kaim G, Braun D, Wüthrich K, Dimroth P (1999) NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles. Eur J Biochem 261:459-467
    • (1999) Eur J Biochem , vol.261 , pp. 459-467
    • Matthey, U.1    Kaim, G.2    Braun, D.3    Wüthrich, K.4    Dimroth, P.5
  • 23
    • 85047698387 scopus 로고    scopus 로고
    • NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/methanol/water (4:4:1)
    • Matthey U, Braun D, Dimroth P (2002) NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/methanol/ water (4:4:1). Eur J Biochem 269:1942-1946
    • (2002) Eur J Biochem , vol.269 , pp. 1942-1946
    • Matthey, U.1    Braun, D.2    Dimroth, P.3
  • 25
    • 0026610872 scopus 로고
    • Heteronuclear 1 H- 15 N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F 1 F 0 ATP synthase: Assignment and secondary structure
    • Norwood TJ, Crawford DA, Steventon ME, Driscoll PC, Campbell ID (1992) Heteronuclear 1 H- 15 N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F 1 F 0 ATP synthase: Assignment and secondary structure. Biochemistry 31:6285-6290
    • (1992) Biochemistry , vol.31 , pp. 6285-6290
    • Norwood, T.J.1    Crawford, D.A.2    Steventon, M.E.3    Driscoll, P.C.4    Campbell, I.D.5
  • 27
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi VK, Girvin ME (1999b) Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402:263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 29
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE (1948) A mathematical theory of communication. Bell Syst Tech J 27:379-423
    • (1948) Bell Syst Tech J , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 30
    • 21244479278 scopus 로고    scopus 로고
    • G-matrix Fourier transform NOESY based protocol for high-quality protein structure determination
    • Shen Y, Atreya HS, Liu G, Szyperski T (2005) G-matrix Fourier transform NOESY based protocol for high-quality protein structure determination. J Am Chem Soc 127:9085-9099
    • (2005) J Am Chem Soc , vol.127 , pp. 9085-9099
    • Shen, Y.1    Atreya, H.S.2    Liu, G.3    Szyperski, T.4
  • 32
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C-Alpha and C-Beta C-13 nuclear-magnetic-resonance chemical shifts
    • Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C-Alpha and C-Beta C-13 nuclear-magnetic-resonance chemical shifts. J Am Chem Soc 113:5490-5492
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 33
    • 33746238247 scopus 로고    scopus 로고
    • Principles and applications of GFT projection NMR spectroscopy
    • Szyperski T, Atreya HS (2006) Principles and applications of GFT projection NMR spectroscopy. Magn Reson Chem 44:S51-S60
    • (2006) Magn Reson Chem , vol.44
    • Szyperski, T.1    Atreya, H.S.2
  • 35
    • 0242657339 scopus 로고    scopus 로고
    • Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR
    • Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH (2003) Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR. FEBS Lett 555:139-143
    • (2003) FEBS Lett , vol.555 , pp. 139-143
    • Tamm, L.K.1    Abildgaard, F.2    Arora, A.3    Blad, H.4    Bushweller, J.H.5
  • 36
    • 0034079112 scopus 로고    scopus 로고
    • Selective constraints, amino acid composition, and the rate of protein evolution
    • Tourasse NJ, Li WH (2000) Selective constraints, amino acid composition, and the rate of protein evolution. Mol Biol Evol 17:656-664
    • (2000) Mol Biol Evol , vol.17 , pp. 656-664
    • Tourasse, N.J.1    Li, W.H.2
  • 37
    • 0141725722 scopus 로고    scopus 로고
    • H-1(C) and H-1(N) total NOE correlations in a single 3D NMR experiment. N-15 and C-13 time-sharing in t(1) and t(2) dimensions for simultaneous data acquisition
    • Xia YL, Yee A, Arrowsmith CH, Gao XL (2003) H-1(C) and H-1(N) total NOE correlations in a single 3D NMR experiment. N-15 and C-13 time-sharing in t(1) and t(2) dimensions for simultaneous data acquisition. J Biomol NMR 27:193-203
    • (2003) J Biomol NMR , vol.27 , pp. 193-203
    • Xia, Y.L.1    Yee, A.2    Arrowsmith, C.H.3    Gao, X.L.4
  • 38
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • Zhang HY, Neal S, Wishart DS (2003) RefDB: A database of uniformly referenced protein chemical shifts. J Biomol NMR 25:173-195
    • (2003) J Biomol NMR , vol.25 , pp. 173-195
    • Zhang, H.Y.1    Neal, S.2    Wishart, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.