ATP synthase b subunit dimerization domain:: A right-handed coiled coil with offset helices

被引：43

作者：

Del Rizzo, Paul A. ^{[1
]}

Bi, Yumin ^{[1
]}

Dunn, Stanley D. ^{[1
]}

机构：

[1] Univ Western Ontario, Dept Biochem, London, ON N6A 5C1, Canada

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2006年 / 364卷 / 04期

基金：

加拿大自然科学与工程研究理事会; 加拿大健康研究院;

关键词：

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

D O I：

10.1016/j.jmb.2006.09.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The dimerization domain of Escherichia coli ATP synthase b subunit forms an atypical parallel two-stranded coiled coil. Sequence analysis reveals an 11-residue abcdefghijk repeat characteristic of right-handed coiled coils, but no other naturally occurring parallel dimeric structure of this class has been identified. The arrangement of the helices was studied by their propensity to form interhelix disulfide linkages and analysis of the stability and shape of disulfide-linked dimers. Disulfides formed preferentially between cysteine residues in an a position of one helix and either of the adjacent h positions of the partner. Such heterodimers were far more stable to thermal denaturation than homodimers and, on the basis of gel-filtration chromatography studies, were similar in shape to both non-covalent dimers and dimers linked through flexible Gly((1-3))CYS C-terminal extensions. The results indicate a right-handed coiled-coil structure with intrinsic asymmetry the two helices being offset rather than in register. A function for the right-handed coiled coil in rotational catalysis is proposed. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：735 / 746

页数：12

共 48 条

[1] Manipulating the length of the b subunit F1 binding domain in F1F0 ATP synthase from Escherichia coli [J].

Bhatt, D ;

Cole, SP ;

Grabar, TB ;

Claggett, SB ;

Cain, BD .

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 2005, 37 (02) :67-74

[2] THE WHEAT CHLOROPLAST GENE FOR CF0 SUBUNIT-I OF ATP SYNTHASE CONTAINS A LARGE INTRON [J].

BIRD, CR ;

KOLLER, B ;

AUFFRET, AD ;

HUTTLY, AK ;

HOWE, CJ ;

DYER, TA ;

GRAY, JC .

EMBO JOURNAL, 1985, 4 (06) :1381-1388

[3] The periplasmic domains of Escherichia coli HflKC oligomerize through right-handed coiled-coil interactions [J].

Briere, Lee-Ann K. ;

Dunn, Stanley D. .

BIOCHEMISTRY, 2006, 45 (28) :8607-8616

[4] Identification of an uncoupling mutation affecting the b subunit of F1F0 ATP synthase in Escherichia coli [J].

Caviston, TL ;

Ketchum, CJ ;

Sorgen, PL ;

Nakamoto, RK ;

Cain, BD .

FEBS LETTERS, 1998, 429 (02) :201-206

[5] Transient accumulation of elastic energy in proton translocating ATP synthase [J].

Cherepanov, DA ;

Mulkidjanian, AY ;

Junge, W .

FEBS LETTERS, 1999, 449 (01) :1-6

[6] Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase -: Deletions disrupt function but not enzyme assembly [J].

Cipriano, DJ ;

Wood, KS ;

Bi, YM ;

Dunn, SD .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (18) :12408-12413

[7] THE ORGANIZATION AND SEQUENCE OF THE GENES FOR ATP SYNTHASE SUBUNITS IN THE CYANOBACTERIUM SYNECHOCOCCUS-6301 - SUPPORT FOR AN ENDOSYMBIOTIC ORIGIN OF CHLOROPLASTS [J].

COZENS, AL ;

WALKER, JE .

JOURNAL OF MOLECULAR BIOLOGY, 1987, 194 (03) :359-383

[8] THE PACKING OF ALPHA-HELICES - SIMPLE COILED-COILS [J].

CRICK, FHC .

ACTA CRYSTALLOGRAPHICA, 1953, 6 (8-9) :689-697

[9] The "second stalk" of Escherichia coli ATP synthase:: structure of the isolated dimerization domain [J].

Del Rizzo, PA ;

Bi, Y ;

Dunn, SD ;

Shilton, BH .

BIOCHEMISTRY, 2002, 41 (21) :6875-6884

[10] On the structure of the stator of the mitochondrial ATP synthase [J].

Dickson, Veronica Kane ;

Silvester, Jocelyn A. ;

Fearnley, Ian M. ;

Leslie, Andrew G. W. ;

Walker, John E. .

EMBO JOURNAL, 2006, 25 (12) :2911-2918

← 1 2 3 4 5 →