 |
PDBsum entry 4p4p
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transferase/DNA
|
PDB id
|
|
|
|
4p4p
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structures of the leishmania infantum polymerase beta.
|
|
|
Authors
|
|
E.Mejia,
M.Burak,
A.Alonso,
V.Larraga,
T.A.Kunkel,
K.Bebenek,
M.Garcia-Diaz.
|
|
|
Ref.
|
|
Dna Repair (amst), 2014,
18,
1-9.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Protozoans of the genus Leishmania, the pathogenic agent causing leishmaniasis,
encode the family X DNA polymerase Li Pol β. Here, we report the first crystal
structures of Li Pol β. Our pre- and post-catalytic structures show that the
polymerase adopts the common family X DNA polymerase fold. However, in contrast
to other family X DNA polymerases, the dNTP-induced conformational changes in Li
Pol β are much more subtle. Moreover, pre- and post-catalytic structures reveal
that Li Pol β interacts with the template strand through a nonconserved,
variable region known as loop3. Li Pol β Δloop3 mutants display a higher
catalytic rate, catalytic efficiency and overall error rates with respect to WT
Li Pol β. These results further demonstrate the subtle structural variability
that exists within this family of enzymes and provides insight into how this
variability underlies the substantial functional differences among their members.
|
|
|
|
|
|
|
