 |
PDBsum entry 1e1r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Atp phosphorylase
|
PDB id
|
|
|
|
1e1r
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
487 a.a.
|
|
|
|
|
|
|
|
|
|
|
467 a.a.
|
|
|
|
|
|
|
|
|
|
|
122 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of bovine mitochondrial f(1)-Atpase inhibited by mg(2+) ADP and aluminium fluoride.
|
|
|
Authors
|
|
K.Braig,
R.I.Menz,
M.G.Montgomery,
A.G.Leslie,
J.E.Walker.
|
|
|
Ref.
|
|
Structure, 2000,
8,
567-573.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
BACKGROUND: The globular domain of the membrane-associated F(1)F(o)-ATP synthase
complex can be detached intact as a water-soluble fragment known as F(1)-ATPase.
It consists of five different subunits, alpha, beta, gamma, delta and epsilon,
assembled with the stoichiometry 3:3:1:1:1. In the crystal structure of bovine
F(1)-ATPase determined previously at 2.8 A resolution, the three catalytic beta
subunits and the three noncatalytic alpha subunits are arranged alternately
around a central alpha-helical coiled coil in the gamma subunit. In the
crystals, the catalytic sites have different nucleotide occupancies. One
contains the triphosphate form of the nucleotide, the second contains the
diphosphate, and the third is unoccupied. Fluoroaluminate complexes have been
shown to mimic the transition state in several ATP and GTP hydrolases. In order
to understand more about its catalytic mechanism, F(1)-ATPase was inhibited with
Mg(2+)ADP and aluminium fluoride and the structure of the inhibited complex was
determined by X-ray crystallography. RESULTS: The structure of bovine
F(1)-ATPase inhibited with Mg(2+)ADP and aluminium fluoride determined at 2.5 A
resolution differs little from the original structure with bound AMP-PNP and
ADP. The nucleotide occupancies of the alpha and beta subunits are unchanged
except that both aluminium trifluoride and Mg(2+)ADP are bound in the
nucleotide-binding site of the beta(DP) subunit. The presence of aluminium
fluoride is accompanied by only minor adjustments in the surrounding protein.
CONCLUSIONS: The structure appears to mimic a possible transition state. The
coordination of the aluminofluoride group has many features in common with other
aluminofluoride-NTP hydrolase complexes. Apparently, once nucleotide is bound to
the catalytic beta subunit, no additional major structural changes are required
for catalysis to occur.
|
|
|
|
|
|
Figure 4.
Figure 4. Location of ADP and fluoroaluminate in the
a[DP]/b[DP] subunit interface. ADP, AlF[3] and the sidechains of
bLys162, bGlu188 (largely hidden), bArg189 and aArg373 are shown
in ball-and-stick representation, using the same atom-colouring
scheme as in Figure 1. The figure was produced using BOBSCRIPT
[32].
|
|
|
|
|
|
The above figure is
reprinted
by permission from Cell Press:
Structure
(2000,
8,
567-573)
copyright 2000.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Structure at 2.8 a resolution of f1-Atpase from bovine heart mitochondria.
|
|
|
Authors
|
|
J.P.Abrahams,
A.G.Leslie,
R.Lutter,
J.E.Walker.
|
|
|
Ref.
|
|
Nature, 1994,
370,
621-628.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #2
|
|
|
Title
|
|
Crystallization of f1-Atpase from bovine heart mitochondria.
|
|
|
Authors
|
|
R.Lutter,
J.P.Abrahams,
M.J.Van raaij,
R.J.Todd,
T.Lundqvist,
S.K.Buchanan,
A.G.Leslie,
J.E.Walker.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
229,
787-790.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Secondary reference #3
|
|
|
Title
|
|
Inherent asymmetry of the structure of f1-Atpase from bovine heart mitochondria at 6.5 a resolution.
|
|
|
Authors
|
|
J.P.Abrahams,
R.Lutter,
R.J.Todd,
M.J.Van raaij,
A.G.Leslie,
J.E.Walker.
|
|
|
Ref.
|
|
Embo J, 1993,
12,
1775-1780.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
