3h4d
Ternary complex of human DNA polymerase iota with template U/T and incoming dGTPTernary complex of human DNA polymerase iota with template U/T and incoming dGTP
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 PubMedHuman DNA polymerase-iota (Poliota) incorporates correct nucleotides opposite template purines with a much higher efficiency and fidelity than opposite template pyrimidines. In fact, the fidelity opposite template T is so poor that Poliota inserts an incorrect dGTP approximately 10 times better than it inserts the correct dATP. We determine here how a template T/U is accommodated in the Poliota active site and why a G is incorporated more efficiently than an A. We show that in the absence of incoming dATP or dGTP (binary complex), template T/U exists in both syn and anti conformations, but in the presence of dATP or dGTP (ternary complexes), template T/U is predominantly in the anti conformation. We also show that dATP and dGTP insert differently opposite template T/U, and that the basis of selection of dGTP over dATP is a hydrogen bond between the N2 amino group of dGTP and Gln59 of Poliota. Replication across template T/U by human DNA polymerase-iota.,Jain R, Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK Structure. 2009 Jul 15;17(7):974-80. PMID:19604477[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
- Homo sapiens
- Aggarwal, A K.
- Jain, R.
- Johnson, R E.
- Nair, D T.
- Prakash, L.
- Prakash, S.
- Dna damage
- Dna polymerase iota
- Dna repair
- Dna replication
- Dna synthesis
- Dna-binding
- Dna-directed dna polymerase
- Magnesium
- Metal-binding
- Mutator protein
- Nucleotidyltransferase
- Nucleus
- Replication
- Replication-dna complex
- Schiff base
- Transferase