3H4D
Ternary complex of human DNA polymerase iota with template U/T and incoming dGTP
Summary for 3H4D
Entry DOI | 10.2210/pdb3h4d/pdb |
Related | 3H40 3H4B |
Descriptor | DNA polymerase iota, 5'-D(*AP*GP*GP*AP*CP*CP*(DOC)), 5'-D(*TP*(BRU)P*GP*GP*GP*TP*CP*CP*T), ... (6 entities in total) |
Functional Keywords | dna polymerase iota, replication, dna damage, dna repair, dna replication, dna synthesis, dna-binding, dna-directed dna polymerase, magnesium, metal-binding, mutator protein, nucleotidyltransferase, nucleus, schiff base, transferase, replication-dna complex, replication/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q9UNA4 |
Total number of polymer chains | 3 |
Total formula weight | 49486.92 |
Authors | Jain, R.,Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. (deposition date: 2009-04-18, release date: 2009-07-21, Last modification date: 2023-09-06) |
Primary citation | Jain, R.,Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. Replication across template T/U by human DNA polymerase-iota. Structure, 17:974-980, 2009 Cited by PubMed Abstract: Human 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. PubMed: 19604477DOI: 10.1016/j.str.2009.04.011 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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