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Dpo4 extension ternary complex with oxoG(anti)-T(anti) pairDpo4 extension ternary complex with oxoG(anti)-T(anti) pair
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed7,8-Dihydro-8-oxoguanine (oxoG), the predominant oxidative DNA damage lesion, is processed differently by high-fidelity and Y-family lesion bypass polymerases. Although high-fidelity polymerases extend predominantly from an A base opposite an oxoG, the Y-family polymerases Dpo4 and human Pol eta preferentially extend from the oxoG*C base pair. We have determined crystal structures of extension Dpo4 ternary complexes with oxoG opposite C, A, G, or T and the next nascent base pair. We demonstrate that neither template backbone nor the architecture of the active site is perturbed by the oxoG(anti)*C and oxoG*A pairs. However, the latter manifest conformational heterogeneity, adopting both oxoG(syn)*A(anti) and oxoG(anti)*A(syn) alignment. Hence, the observed reduced primer extension from the dynamically flexible 3'-terminal primer base A is explained. Because of homology between Dpo4 and Pol eta, such a dynamic screening mechanism might be utilized by Dpo4 and Pol eta to regulate error-free versus error-prone bypass of oxoG and other lesions. Impact of conformational heterogeneity of OxoG lesions and their pairing partners on bypass fidelity by Y family polymerases.,Rechkoblit O, Malinina L, Cheng Y, Geacintov NE, Broyde S, Patel DJ Structure. 2009 May 13;17(5):725-36. PMID:19446528[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- DNA-directed DNA polymerase
- Sulfolobus solfataricus p2
- Malinina, L.
- Patel, D J.
- Rechkoblit, O.
- 8-oxoguanine
- Dna damage
- Dna polymerase
- Dna repair
- Dna replication
- Dna-binding
- Dna-directed dna polymerase
- Lesion bypass
- Magnesium
- Metal-binding
- Mutator protein
- Nucleotidyltransferase
- Transferase
- Transferase-dna complex
- Y-family