Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3KNT

Crystal structure of Methanocaldococcus jannaschii 8-oxoguanine glycosylase/lyase in complex with 15mer DNA containing 8-oxoguanine

Summary for 3KNT
Entry DOI10.2210/pdb3knt/pdb
DescriptorN-glycosylase/DNA lyase, 5'-D(*AP*CP*GP*TP*CP*CP*AP*(8OG)P*GP*TP*CP*TP*AP*CP*C)-3', 5'-D(*TP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*G)-3', ... (5 entities in total)
Functional Keywordsprotein-dna complex, ogg, helix-hairpin-helix, glycosylase, 8-oxoguanine, 8-oxog, dna repair, dna damage, glycosidase, multifunctional enzyme, nuclease, hydrolase, lyase-dna complex, lyase/dna
Biological sourceMethanocaldococcus jannaschii (Methanococcus jannaschii)
More
Total number of polymer chains12
Total formula weight136351.04
Authors
Faucher, F.,Doublie, S. (deposition date: 2009-11-12, release date: 2010-02-02, Last modification date: 2023-09-06)
Primary citationFaucher, F.,Wallace, S.S.,Doublie, S.
The C-terminal Lysine of Ogg2 DNA Glycosylases is a Major Molecular Determinant for Guanine/8-Oxoguanine Distinction.
J.Mol.Biol., 397:46-56, 2010
Cited by
PubMed Abstract: 7,8-Dihydro-8-oxoguanine (8-oxoG) is a major oxidative lesion found in DNA. The 8-oxoguanine DNA glycosylases (Ogg) responsible for the removal of 8-oxoG are divided into three families Ogg1, Ogg2 and AGOG. The Ogg2 members are devoid of the recognition loop used by Ogg1 to discriminate between 8-oxoG and guanine and it was unclear until recently how Ogg2 enzymes recognize the oxidized base. We present here the first crystallographic structure of an Ogg2 member, Methanocaldococcus janischii Ogg, in complex with a DNA duplex containing the 8-oxoG lesion. This structure highlights the crucial role of the C-terminal lysine, strictly conserved in Ogg2, in the recognition of 8-oxoG. The structure also reveals that Ogg2 undergoes a conformational change upon DNA binding similar to that observed in Ogg1 glycosylases. Furthermore, this work provides a structural rationale for the lack of opposite base specificity in this family of enzymes.
PubMed: 20083120
DOI: 10.1016/j.jmb.2010.01.024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon