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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 DOI10.2210/pdb3mby/pdb
DescriptorDNA 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 Keywordsnucleotidyl transferase, dna polymerase, a:(syn)8oxodgtp, a:c transversion, transferase, lyase-dna complex, lyase/dna
Biological sourceHomo sapiens (human)
Cellular locationNucleus: P06746
Total number of polymer chains4
Total formula weight48398.68
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 citationBatra, 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: 20526335
DOI: 10.1038/nsmb.1852
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

226707

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