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Structures of the Leishmania infantum polymerase beta.
Mejia, Edison; Burak, Matthew; Alonso, Ana; Larraga, Vicente; Kunkel, Thomas A; Bebenek, Katarzyna; Garcia-Diaz, Miguel.
Afiliación
  • Mejia E; Department of Pharmacological Sciences, Stony Brook University, BST 7-169, Stony Brook, NY 11794-8651, USA.
  • Burak M; Department of Pharmacological Sciences, Stony Brook University, BST 7-169, Stony Brook, NY 11794-8651, USA.
  • Alonso A; Centro de Investigaciones Biologicas, CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain.
  • Larraga V; Centro de Investigaciones Biologicas, CSIC, Ramiro de Maeztu 9, 28040 Madrid, Spain.
  • Kunkel TA; Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709, USA.
  • Bebenek K; Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709, USA. Electronic address: bebenek@niehs.nih.gov.
  • Garcia-Diaz M; Department of Pharmacological Sciences, Stony Brook University, BST 7-169, Stony Brook, NY 11794-8651, USA. Electronic address: miguel.garcia-diaz@stonybrook.edu.
DNA Repair (Amst) ; 18: 1-9, 2014 Jun.
Article en En | MEDLINE | ID: mdl-24666693
Protozoans of the genus Leishmania, the pathogenic agent causing leishmaniasis, encode the family X DNA polymerase Li Pol ß. Here, we report the first crystal structures of Li Pol ß. 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 ß are much more subtle. Moreover, pre- and post-catalytic structures reveal that Li Pol ß interacts with the template strand through a nonconserved, variable region known as loop3. Li Pol ß Δloop3 mutants display a higher catalytic rate, catalytic efficiency and overall error rates with respect to WT Li Pol ß. 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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Leishmania infantum / ADN Polimerasa beta / Dominio Catalítico Tipo de estudio: Prognostic_studies Idioma: En Revista: DNA Repair (Amst) Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Leishmania infantum / ADN Polimerasa beta / Dominio Catalítico Tipo de estudio: Prognostic_studies Idioma: En Revista: DNA Repair (Amst) Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Países Bajos