2024-03-28T17:26:01Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/2117452021-11-22T12:51:16Zcom_10261_86com_10261_1col_10261_339
00925njm 22002777a 4500
dc
Mejía Edison
author
Burak, Matthew
author
Alonso, Ana
author
Larraga, Vicente
author
Kunkel, Thomas A.
author
Bebenek, Katarzyna
author
García-Díaz, Miguel
author
2014-06
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.
DNA Repair (Amst) 18:1-9 (2014)
1568-7864
http://hdl.handle.net/10261/211745
10.1016/j.dnarep.2014.03.001
1568-7856
http://dx.doi.org/10.13039/100000002
http://dx.doi.org/10.13039/100008054
24666693
DNA repair
Leishmaniasis
DNA polymerase
Family X
Structures of the Leishmania infantum polymerase beta