 |
PDBsum entry 1jbb
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Molecular insights into polyubiquitin chain assembly: crystal structure of the mms2/ubc13 heterodimer.
|
 |
|
Authors
|
 |
A.P.Vandemark,
R.M.Hofmann,
C.Tsui,
C.M.Pickart,
C.Wolberger.
|
 |
|
Ref.
|
 |
Cell, 2001,
105,
711-720.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
While the signaling properties of ubiquitin depend on the topology of
polyubiquitin chains, little is known concerning the molecular basis of
specificity in chain assembly and recognition. UEV/Ubc complexes have been
implicated in the assembly of Lys63-linked polyubiquitin chains that act as a
novel signal in postreplicative DNA repair and I kappa B alpha kinase
activation. The crystal structure of the Mms2/Ubc13 heterodimer shows the active
site of Ubc13 at the intersection of two channels that are potential binding
sites for the two substrate ubiquitins. Mutations that destabilize the
heterodimer interface confer a marked UV sensitivity, providing direct evidence
that the intact heterodimer is necessary for DNA repair. Selective mutations in
the channels suggest a molecular model for specificity in the assembly of
Lys63-linked polyubiquitin signals.
|
 |
 |
 |
|
 |
|
 |
Figure 2.
Figure 2. The Mms2/Ubc13 Binding Interface Contains Both
Hydrophobic and Polar Surfaces(A) Mms2/Ubc13 heterodimerization
interface. Ubc13 is displayed as a surface with Mms2 interface
residues in light blue.(B) F8A-Mms2 (light blue) environment
showing hydrophobic contacts with Ubc13 residues E55, L56, Y57,
and R70 (green). The Ubc13 backbone is shown in green.(C)
E55-Ubc13 environment highlighting hydrogen bonds that bridge
the interface (black). The Mms2 backbone shown in blue, the
Ubc13 backbone in green
|
 |
Figure 4.
Figure 4. Channels and Interfering MutationsThe heterodimer
is shown as a surface. The three channels referred to in the
text are colored green and numbered, interfering mutations are
shown in blue. Ubc13-Cys87 is shown in yellow. The figure was
generated with VMD (Humphrey et al., 1996) and RENDER (Merritt
and Bacon, 1997)
|
 |
|
 |
 |
|
The above figures are
reprinted
by permission from Cell Press:
Cell
(2001,
105,
711-720)
copyright 2001.
|
 |
|
|
|
|
 |