 |
PDBsum entry 3a5c
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
561 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
450 a.a.
|
|
|
|
|
|
|
|
|
|
|
129 a.a.
|
|
|
|
|
|
|
|
|
|
|
104 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Inter-Subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-Atpase.
|
|
|
Authors
|
|
N.Numoto,
Y.Hasegawa,
K.Takeda,
K.Miki.
|
|
|
Ref.
|
|
Embo Rep, 2009,
10,
1228-1234.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase
complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation
scheme, architecture and subunit composition. However, there is no detailed
structural information on V-ATPases despite the abundant biochemical and
biophysical research. Here, we report a crystallographic study of V1-ATPase,
from Thermus thermophilus, which is a soluble component consisting of A, B, D
and F subunits. The structure at 4.5 A resolution reveals inter-subunit
interactions and nucleotide binding. In particular, the structure of the central
stalk composed of D and F subunits was shown to be characteristic of V1-ATPases.
Small conformational changes of respective subunits and significant
rearrangement of the quaternary structure observed in the three AB pairs were
related to the interaction with the straight central stalk. The rotation
mechanism is discussed based on a structural comparison between V1-ATPases and
F1-ATPases.
|
|
|
|
|
|
|
