 |
PDBsum entry 1be3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
1be3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
446 a.a.
|
|
|
|
|
|
|
|
|
|
|
419 a.a.
|
|
|
|
|
|
|
|
|
|
|
379 a.a.
|
|
|
|
|
|
|
|
|
|
|
241 a.a.
|
|
|
|
|
|
|
|
|
|
|
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
106 a.a.
|
|
|
|
|
|
|
|
|
|
|
81 a.a.
|
|
|
|
|
|
|
|
|
|
|
64 a.a.
|
|
|
|
|
|
|
|
|
|
|
33 a.a.
|
|
|
|
|
|
|
|
|
|
|
62 a.a.
|
|
|
|
|
|
|
|
|
|
|
22 a.a.
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Complete structure of the 11-Subunit bovine mitochondrial cytochrome bc1 complex.
|
|
|
Authors
|
|
S.Iwata,
J.W.Lee,
K.Okada,
J.K.Lee,
M.Iwata,
B.Rasmussen,
T.A.Link,
S.Ramaswamy,
B.K.Jap.
|
|
|
Ref.
|
|
Science, 1998,
281,
64-71.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory
multienzyme complex and it recognizes a mitochondrial targeting presequence.
Refined crystal structures of the 11-subunit bc1 complex from bovine heart
reveal full views of this bifunctional enzyme. The "Rieske"
iron-sulfur protein subunit shows significant conformational changes in
different crystal forms, suggesting a new electron transport mechanism of the
enzyme. The mitochondrial targeting presequence of the "Rieske"
protein (subunit 9) is lodged between the two "core" subunits at the
matrix side of the complex. These "core" subunits are related to the
matrix processing peptidase, and the structure unveils how mitochondrial
targeting presequences are recognized.
|
|
|
|
|
|
|
|
Figure 3.
Fig. 3. Interaction of the mitochondrial targeting
presequence of the ISP (subunit 9 in bright red) with the two
core subunits (core^ 1 in aqua blue and core 2 in green). (A)
Position of subunit 9 between the core 1 and core 2 subunits
viewed from the mitochondrial matrix side of the complex. The
cleaved NH[2]-terminal arm of the^ ISP is shown in magenta. The
 -sheet of
the NH[2]-terminal domain of core 2 is highlighted (yellowish
green), and the two possible^ Zn2+-binding sites are marked by
black arrowheads. (B) Stereoview of various interactions between
the COOH-terminal -strand of^
subunit 9 and its binding site in the core 2 subunit.
|
|
Figure 4.
Fig. 4. Structural comparison of the ISP in P6[5]22 and P6[5]
crystal forms of bovine cytochrome bc[1]. Stereoview of the
superimposed ISP functional domains at "c[1]" (red) and "Int"
(blue) positional states using the base folds. The
cluster-binding folds are shown in saturated^ colors, whereas
the base folds are shown in pale colors. These^ structures are
related by a hinge motion and the isomerization of Pro175 near
the [2Fe-2S] center.
|
|
|
|
|
|
The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
281,
64-71)
copyright 1998.
|
|
|
|
|
|
|
