3MBY
Ternary complex of DNA Polymerase BETA with template base A and 8oxodGTP in the active site with a dideoxy terminated primer
Summary for 3MBY
Entry DOI | 10.2210/pdb3mby/pdb |
Descriptor | DNA polymerase beta, DNA (5'-D(*CP*CP*GP*AP*CP*AP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3'), DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*(DOC))-3'), ... (9 entities in total) |
Functional Keywords | nucleotidyl transferase, dna polymerase, a:(syn)8oxodgtp, a:c transversion, transferase, lyase-dna complex, lyase/dna |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: P06746 |
Total number of polymer chains | 4 |
Total formula weight | 48398.68 |
Authors | Batra, V.K.,Beard, W.A.,Hou, E.W.,Pedersen, L.C.,Prasad, R.,Wilson, S.H. (deposition date: 2010-03-26, release date: 2010-06-09, Last modification date: 2023-09-06) |
Primary citation | Batra, V.K.,Beard, W.A.,Hou, E.W.,Pedersen, L.C.,Prasad, R.,Wilson, S.H. Mutagenic conformation of 8-oxo-7,8-dihydro-2'-dGTP in the confines of a DNA polymerase active site. Nat.Struct.Mol.Biol., 17:889-890, 2010 Cited by PubMed Abstract: The major product of oxidative base damage is 8-oxo-7,8-dihydro-2'-deoxyguanine (8odG). The coding potential of this lesion is modulated by its glycosidic torsion angle that controls whether its Watson-Crick or Hoogsteen edge is used for base pairing. The 2.0-A structure of DNA polymerase (pol) beta bound with 8odGTP opposite template adenine indicates that the modified nucleotide assumes the mutagenic syn conformation and that the nonmutagenic anti conformation would be incompatible with efficient DNA synthesis. PubMed: 20526335DOI: 10.1038/nsmb.1852 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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