3SAV

MUTM Slanted complex 8

Summary for 3SAV

• Entry DOI: 10.2210/pdb3sav/pdb
• Related: 3SAR 3SAS 3SAT 3SAU 3SAW 3SBJ
• Descriptor: DNA GLYCOSYLASE, DNA (5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*AP*AP*GP*GP*AP*CP*GP*C)-3'), DNA (5'-D(*TP*GP*CP*GP*T*CP*CP*TP*TP*GP*TP*(CX2)P*TP*AP*CP*C)-3'), ... (5 entities in total)
• Functional Keywords: dna glycosylase, dna repair, damage search, translocation, disulfide crosslinking, dna damage, dna-binding, glycosidase, hydrolase, lyase, metal-binding, multifunctional enzyme, zinc-finger, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus (Bacillus stearothermophilus); More
• Total number of polymer chains: 3
• Total formula weight: 40505.24

Authors

Spong, M.C.,Qi, Y.,Verdine, G.L. (deposition date: 2011-06-03, release date: 2012-01-11, Last modification date: 2023-09-13)

Primary citation

Qi, Y.,Nam, K.,Spong, M.C.,Banerjee, A.,Sung, R.J.,Zhang, M.,Karplus, M.,Verdine, G.L.
Strandwise translocation of a DNA glycosylase on undamaged DNA.
Proc.Natl.Acad.Sci.USA, 109:1086-1091, 2012

PubMed Abstract: Base excision repair of genotoxic nucleobase lesions in the genome is critically dependent upon the ability of DNA glycosylases to locate rare sites of damage embedded in a vast excess of undamaged DNA, using only thermal energy to fuel the search process. Considerable interest surrounds the question of how DNA glycosylases translocate efficiently along DNA while maintaining their vigilance for target damaged sites. Here, we report the observation of strandwise translocation of 8-oxoguanine DNA glycosylase, MutM, along undamaged DNA. In these complexes, the protein is observed to translocate by one nucleotide on one strand while remaining untranslocated on the complementary strand. We further report that alterations of single base-pairs or a single amino acid substitution (R112A) can induce strandwise translocation. Molecular dynamics simulations confirm that MutM can translocate along DNA in a strandwise fashion. These observations reveal a previously unobserved mode of movement for a DNA-binding protein along the surface of DNA.

PubMed: 22219368
DOI: 10.1073/pnas.1111237108

Experimental method

X-RAY DIFFRACTION (2.125 Å)