메뉴 건너뛰기




Volumn 364, Issue 4, 2006, Pages 735-746

ATP Synthase b Subunit Dimerization Domain: A Right-Handed Coiled Coil with Offset Helices

Author keywords

ATP synthase; hendecad repeat; molecular motor; peripheral stalk; right handed coiled coil

Indexed keywords

CYSTEINE; DIMER; DISULFIDE; GLYCINE; HOMODIMER; MOLECULAR MOTOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 33750951013     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.028     Document Type: Article
Times cited : (48)

References (48)
  • 1
    • 26844533433 scopus 로고    scopus 로고
    • Rotary molecular motors
    • Wilkens S. Rotary molecular motors. Advan. Protein Chem. 71 (2005) 345-382
    • (2005) Advan. Protein Chem. , vol.71 , pp. 345-382
    • Wilkens, S.1
  • 2
    • 33744961816 scopus 로고    scopus 로고
    • The ATP synthase: parts and properties of a rotary motor
    • Hackney D.D., and Tamanoi F. (Eds), Elsevier Academic Press, New York
    • Duncan T.M. The ATP synthase: parts and properties of a rotary motor. In: Hackney D.D., and Tamanoi F. (Eds). The Enzymes: Energy Coupling and Molecular Motors. 3rd edit. vol. 23 (2004), Elsevier Academic Press, New York 203-275
    • (2004) The Enzymes: Energy Coupling and Molecular Motors. 3rd edit. , vol.23 , pp. 203-275
    • Duncan, T.M.1
  • 4
    • 0021879552 scopus 로고
    • Nucleotide sequence of the Rhodospirillum rubrum atp operon
    • Falk G., Hampe A., and Walker J.E. Nucleotide sequence of the Rhodospirillum rubrum atp operon. Biochem. J. 228 (1985) 391-407
    • (1985) Biochem. J. , vol.228 , pp. 391-407
    • Falk, G.1    Hampe, A.2    Walker, J.E.3
  • 7
    • 0023644688 scopus 로고
    • The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin of chloroplasts
    • Cozens A.L., and Walker J.E. The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin of chloroplasts. J. Mol. Biol. 194 (1987) 359-383
    • (1987) J. Mol. Biol. , vol.194 , pp. 359-383
    • Cozens, A.L.1    Walker, J.E.2
  • 9
    • 0035830452 scopus 로고    scopus 로고
    • Specific heterodimer formation by the cytoplasmic domains of the b and b' subunits of cyanobacterial ATP synthase
    • Dunn S.D., Kellner E., and Lill H. Specific heterodimer formation by the cytoplasmic domains of the b and b' subunits of cyanobacterial ATP synthase. Biochemistry 40 (2001) 187-192
    • (2001) Biochemistry , vol.40 , pp. 187-192
    • Dunn, S.D.1    Kellner, E.2    Lill, H.3
  • 10
    • 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 D.T., Bestard J.A., and Dunn S.D. The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions. J. Biol. Chem. 273 (1998) 15162-15168
    • (1998) J. Biol. Chem. , vol.273 , pp. 15162-15168
    • McLachlin, D.T.1    Bestard, J.A.2    Dunn, S.D.3
  • 11
    • 0032491567 scopus 로고    scopus 로고
    • 1 via an δ-subunit in the Escherichia coli ATP synthase
    • 1 via an δ-subunit in the Escherichia coli ATP synthase. J. Biol. Chem. 273 (1998) 29406-29410
    • (1998) J. Biol. Chem. , vol.273 , pp. 29406-29410
    • Rodgers, A.J.1    Capaldi, R.A.2
  • 14
    • 33748986212 scopus 로고    scopus 로고
    • ATP synthase: Subunit-subunit interactions in the stator stalk
    • Weber J. ATP synthase: Subunit-subunit interactions in the stator stalk. Biochim. Biophys. Acta 1575 (2006) 1162-1170
    • (2006) Biochim. Biophys. Acta , vol.1575 , pp. 1162-1170
    • Weber, J.1
  • 15
    • 84954238731 scopus 로고    scopus 로고
    • ATP Synthase stalk subunits b, δ, and ε: structures and functions in energy coupling
    • Futai M., and Wada Y. (Eds), Springer-Verlag, Weinheim
    • Dunn S.D., Cipriano D.J., and Del Rizzo P.A. ATP Synthase stalk subunits b, δ, and ε: structures and functions in energy coupling. In: Futai M., and Wada Y. (Eds). Handbook of ATPases (2004), Springer-Verlag, Weinheim 311-338
    • (2004) Handbook of ATPases , pp. 311-338
    • Dunn, S.D.1    Cipriano, D.J.2    Del Rizzo, P.A.3
  • 16
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker J.E., and Dickson V.K. The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757 (2006) 286-296
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 20
    • 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
  • 24
    • 33744949445 scopus 로고    scopus 로고
    • Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly
    • Cipriano D.J., Wood K.S., Bi Y., and Dunn S.D. Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly. J. Biol. Chem. 281 (2006) 12408-12413
    • (2006) J. Biol. Chem. , vol.281 , pp. 12408-12413
    • Cipriano, D.J.1    Wood, K.S.2    Bi, Y.3    Dunn, S.D.4
  • 25
    • 0000920828 scopus 로고
    • The packing of α-helices: simple coiled-coils
    • Crick F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallog. 6 (1953) 689-697
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 26
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., Klemm J.D., Kim P.S., and Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254 (1991) 539-544
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 27
    • 0032514952 scopus 로고    scopus 로고
    • Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in alpha-helical coiled-coils
    • Kohn W.D., Kay C.M., and Hodges R.S. Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in alpha-helical coiled-coils. J. Mol. Biol. 283 (1998) 993-1012
    • (1998) J. Mol. Biol. , vol.283 , pp. 993-1012
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 28
    • 0032546758 scopus 로고    scopus 로고
    • Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids
    • Krylov D., Barchi J., and Vinson C. Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids. J. Mol. Biol. 279 (1998) 959-972
    • (1998) J. Mol. Biol. , vol.279 , pp. 959-972
    • Krylov, D.1    Barchi, J.2    Vinson, C.3
  • 29
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: new structures and new functions
    • Lupas A. Coiled coils: new structures and new functions. Trends Biochem. Sci. 21 (1996) 375-382
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 30
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson D.N. The design of coiled-coil structures and assemblies. Advan. Protein Chem. 70 (2005) 79-112
    • (2005) Advan. Protein Chem. , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 31
    • 17444424974 scopus 로고    scopus 로고
    • The structure of α-helical coiled coils
    • Lupas A.N., and Gruber M. The structure of α-helical coiled coils. Advan. Protein. Chem. 70 (2005) 37-78
    • (2005) Advan. Protein. Chem. , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 34
    • 0032805887 scopus 로고    scopus 로고
    • The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
    • Nooren I.M., Kaptein R., Sauer R.T., and Boelens R. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nature Struct. Biol. 6 (1999) 755-759
    • (1999) Nature Struct. Biol. , vol.6 , pp. 755-759
    • Nooren, I.M.1    Kaptein, R.2    Sauer, R.T.3    Boelens, R.4
  • 35
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • Harbury P.B., Plecs J.J., Tidor B., Alber T., and Kim P.S. High-resolution protein design with backbone freedom. Science 282 (1998) 1462-1467
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber, T.4    Kim, P.S.5
  • 36
    • 23144450570 scopus 로고    scopus 로고
    • REPPER-repeats and their periodicities in fibrous proteins
    • Gruber M., Soding J., and Lupas A.N. REPPER-repeats and their periodicities in fibrous proteins. Nucl. Acids Res. 33 (2005) W239-W243
    • (2005) Nucl. Acids Res. , vol.33
    • Gruber, M.1    Soding, J.2    Lupas, A.N.3
  • 39
    • 0034616959 scopus 로고    scopus 로고
    • Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d"
    • Tripet B., Wagschal K., Lavigne P., Mant C.T., and Hodges R.S. Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d". J. Mol. Biol. 300 (2000) 377-402
    • (2000) J. Mol. Biol. , vol.300 , pp. 377-402
    • Tripet, B.1    Wagschal, K.2    Lavigne, P.3    Mant, C.T.4    Hodges, R.S.5
  • 40
    • 1342268069 scopus 로고    scopus 로고
    • Defining the minimum size of a hydrophobic cluster in two-stranded α-helical coiled-coils: effects on protein stability
    • Lu S.M., and Hodges R.S. Defining the minimum size of a hydrophobic cluster in two-stranded α-helical coiled-coils: effects on protein stability. Protein Sci. 13 (2004) 714-726
    • (2004) Protein Sci. , vol.13 , pp. 714-726
    • Lu, S.M.1    Hodges, R.S.2
  • 42
    • 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 D.T., Coveny A.M., Clark S.M., and Dunn S.D. Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase. J. Biol. Chem. 275 (2000) 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
  • 44
    • 0032947857 scopus 로고    scopus 로고
    • Transient accumulation of elastic energy in proton translocating ATP synthase
    • Cherepanov D.A., Mulkidjanian A.Y., and Junge W. Transient accumulation of elastic energy in proton translocating ATP synthase. FEBS Letters 449 (1999) 1-6
    • (1999) FEBS Letters , vol.449 , pp. 1-6
    • Cherepanov, D.A.1    Mulkidjanian, A.Y.2    Junge, W.3
  • 46
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro M.M., and Bolen D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27 (1988) 8063-8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 47
    • 0027489832 scopus 로고
    • Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation
    • Swint L., and Robertson A.D. Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci. 2 (1993) 2037-2049
    • (1993) Protein Sci. , vol.2 , pp. 2037-2049
    • Swint, L.1    Robertson, A.D.2
  • 48
    • 33746063714 scopus 로고    scopus 로고
    • The periplasmic domains of Escherichia coli HflKC oligomerize through right-handed coiled-coil interactions
    • Briere L.K., and Dunn S.D. The periplasmic domains of Escherichia coli HflKC oligomerize through right-handed coiled-coil interactions. Biochemistry 45 (2006) 8607-8616
    • (2006) Biochemistry , vol.45 , pp. 8607-8616
    • Briere, L.K.1    Dunn, S.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.