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Volumn 106, Issue 51, 2009, Pages 21597-21601

The structure of the membrane extrinsic region of bovine ATP synthase

Author keywords

Mitochondria; Rotational catalysis; Stator

Indexed keywords

MITOCHONDRIAL PROTEIN; OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SELENOMETHIONINE; UNCLASSIFIED DRUG;

EID: 76049093135     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910365106     Document Type: Article
Times cited : (148)

References (33)
  • 1
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • Rubinstein JL, Walker JE, Henderson R (2003) Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J 22:6182-6192.
    • (2003) EMBO J , vol.22 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 3
    • 33751294565 scopus 로고    scopus 로고
    • Inhibitors of the catalytic domain of mitochondrial ATP synthase
    • Gledhill JR, Walker JE (2006) Inhibitors of the catalytic domain of mitochondrial ATP synthase. Biochem Soc Trans 34:989-992.
    • (2006) Biochem Soc Trans , vol.34 , pp. 989-992
    • Gledhill, J.R.1    Walker, J.E.2
  • 5
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AGW, Walker JE (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286:1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 6
    • 0027943885 scopus 로고
    • 1-ATPase and in its absence
    • 1-ATPase and in its absence J Mol Biol 242:408-421.
    • (1994) J Mol Biol , vol.242 , pp. 408-421
    • Collinson, I.R.1
  • 7
    • 33947585115 scopus 로고    scopus 로고
    • o-ATP synthase interacts with the N-terminal region of an α subunit
    • o-ATP synthase interacts with the N-terminal region of an α subunit. J Mol Biol 368:310-318.
    • (2007) J Mol Biol , vol.368 , pp. 310-318
    • Carbajo, R.J.1
  • 9
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker JE, Dickson VK (2006) The peripheral stalk of the mitochondrial ATP synthase. Biochim Biophys Acta 1757:286-296.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 14
    • 0343472078 scopus 로고    scopus 로고
    • o interactions require a local α-helix at the C-terminal end of the subunit
    • o interactions require a local α-helix at the C-terminal end of the subunit. Biochemistry 36:10936-10943.
    • (1997) Biochemistry , vol.36 , pp. 10936-10943
    • Joshi, S.1    Gong, J.2    Nath, C.3    Shah, J.4
  • 15
    • 0036971192 scopus 로고    scopus 로고
    • ATP synthase from Saccharomyces cerevisiae: Location of the OSCP subunit in the peripheral stalk region
    • Rubinstein J, Walker JE (2002) ATP synthase from Saccharomyces cerevisiae: Location of the OSCP subunit in the peripheral stalk region. J Mol Biol 321:613-619.
    • (2002) J Mol Biol , vol.321 , pp. 613-619
    • Rubinstein, J.1    Walker, J.E.2
  • 17
    • 0032511038 scopus 로고    scopus 로고
    • The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions
    • McLachlin DT, Bestard JA, Dunn SD (1998) The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions. J Biol Chem 273:15162-15168.
    • (1998) J Biol Chem , vol.273 , pp. 15162-15168
    • McLachlin, D.T.1    Bestard, J.A.2    Dunn, S.D.3
  • 18
    • 0032502352 scopus 로고    scopus 로고
    • 2δ complex from Escherichia coli ATP synthase
    • 2δ complex from Escherichia coli ATP synthase. J Biol Chem 273:8646-8651.
    • (1998) J Biol Chem , vol.273 , pp. 8646-8651
    • Dunn, S.D.1    Chandler, J.2
  • 19
    • 0034625459 scopus 로고    scopus 로고
    • Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase
    • McLachlin DT, Coveny AM, Clark SM, Dunn SD (2000) Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase. J Biol Chem 275:17571-17577.
    • (2000) J Biol Chem , vol.275 , pp. 17571-17577
    • McLachlin, D.T.1    Coveny, A.M.2    Clark, S.M.3    Dunn, S.D.4
  • 20
    • 0742270832 scopus 로고    scopus 로고
    • 1-ATPase
    • 1-ATPase. Nature 427:465-468.
    • (2004) Nature , vol.427 , pp. 465-468
    • Itoh, H.1
  • 22
    • 0038719727 scopus 로고    scopus 로고
    • A unique resting position of the ATP-synthase from chloroplasts
    • Mellwig C, Böttcher B (2003) A unique resting position of the ATP-synthase from chloroplasts. J Biol Chem 278:18544-18549.
    • (2003) J Biol Chem , vol.278 , pp. 18544-18549
    • Mellwig, C.1    Böttcher, B.2
  • 26
    • 76049098629 scopus 로고    scopus 로고
    • Leslie AGW (1992). Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography 26.
    • Leslie AGW (1992). Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 and ESF-EAMCB Newsletter on Protein Crystallography 26.
  • 27
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans PR (2005) Scaling and assessment of data quality. Acta Crystallogr D 62:72-82.
    • (2005) Acta Crystallogr D , vol.62 , pp. 72-82
    • Evans, P.R.1
  • 28
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French G, Wilson K (1978). On the treatment of negative intensity observations. Acta Crystallogr A 34:517-525.
    • (1978) Acta Crystallogr A , vol.34 , pp. 517-525
    • French, G.1    Wilson, K.2
  • 30
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) COOT: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 32
    • 76049094011 scopus 로고    scopus 로고
    • Afonine PV, Grosse-Kunstleve RW, Adams PD (2005) The Phenix refinement framework. CCP4 Newsletter on Protein Crystallography 42, contribution 8.
    • Afonine PV, Grosse-Kunstleve RW, Adams PD (2005) The Phenix refinement framework. CCP4 Newsletter on Protein Crystallography 42, contribution 8.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.