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PDBsum entry 1ohh
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487 a.a.
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469 a.a.
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94 a.a.
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37 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of bovine f1-Atpase in complex with its regulatory protein if1.
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Authors
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E.Cabezón,
M.G.Montgomery,
A.G.Leslie,
J.E.Walker.
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Ref.
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Nat Struct Biol, 2003,
10,
744-750.
[DOI no: ]
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PubMed id
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Abstract
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In mitochondria, the hydrolytic activity of ATP synthase is prevented by an
inhibitor protein, IF1. The active bovine protein (84 amino acids) is an
alpha-helical dimer with monomers associated via an antiparallel alpha-helical
coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in
the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal
structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind
in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central
gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP)
and beta(DP) subunits relative to previous structures. The presence of ATP in
the catalytic site of the beta(DP) subunit implies that the inhibited state
represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
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Figure 3.
Figure 3. Stereo view of the contacts between F[1]-ATPase and
IF[1]. Side chains from residues involved in contacts between
F[1]-ATPase and IF[1] have been drawn. For details of the color
scheme see the legend to Figure 1.
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Figure 6.
Figure 6. The inhibition of the ATP hydrolytic activity of ATP
synthase by IF[1]. The scheme is based on the binding change
mechanism of ATP hydrolysis26. See text for further details.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
744-750)
copyright 2003.
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Secondary reference #1
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Title
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Structure at 2.8 a resolution of f1-Atpase from bovine heart mitochondria.
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Authors
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J.P.Abrahams,
A.G.Leslie,
R.Lutter,
J.E.Walker.
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Ref.
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Nature, 1994,
370,
621-628.
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PubMed id
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Secondary reference #2
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Title
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Crystallization of f1-Atpase from bovine heart mitochondria.
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Authors
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R.Lutter,
J.P.Abrahams,
M.J.Van raaij,
R.J.Todd,
T.Lundqvist,
S.K.Buchanan,
A.G.Leslie,
J.E.Walker.
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Ref.
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J Mol Biol, 1993,
229,
787-790.
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PubMed id
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Secondary reference #3
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Title
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The structure of bovine if(1), The regulatory subunit of mitochondrial f-Atpase.
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Authors
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E.Cabezón,
M.J.Runswick,
A.G.Leslie,
J.E.Walker.
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Ref.
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EMBO J, 2001,
20,
6990-6996.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Crystal structure of bovine IF[1]-H49K. (A) Stereo view
of the 2.2 Å resolution 2F[o] - F[c] electron density map
calculated with CNS (contoured at 1.5  )
from residues 27 to 41 of the protein. (B) Stereo view of the
crystallographic packing. The four IF[1] monomers in the
asymmetric unit (A -D) are represented in red, sky blue, yellow
and dark blue, respectively. The origin of the unit cell and the
a, b and c axes are labelled 'o', 'a', 'b' and 'c',
respectively. (C) View along the crystallographic b-axis. (D)
Interactions between the two types of dimers. Dashed lines
represent the minimal inhibitory sequence of IF[1], which are
masked in the tetramers. C- and N-termini are indicated with the
letters C and N, respectively.
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Figure 2.
Figure 2 Interhelical packing in IF[1]-H49K structure. (A)
Ribbon diagram of the active dimer. Dashed lines represent the
minimal inhibitory sequence. The disordered N-terminal residues
1 -18 are shown as dotted lines. (B) Schematic representation of
the interhelical packing. Residues involved in forming the
coiled coils are represented with their sequence number. Helices
are coloured as in Figure 1. Dotted lines represent the
continuity of the helices. The position of lysine 49 in helix C
(yellow) is shown in black, indicating the contacts with helices
B (sky blue) and D (dark blue). Dashed boxes show the two areas
of the protein represented in more detail in (C) and (D). (C)
Stereo view of the interhelical packing in the N-terminus of the
protein. (D) Stereo view of the interhelical packing in the
C-terminus of the AB dimer.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by Macmillan Publishers Ltd
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