2F5S

Catalytically inactive (E3Q) MutM crosslinked to oxoG:C containing DNA CC1

Summary for 2F5S

• Entry DOI: 10.2210/pdb2f5s/pdb
• Related: 1L1T 1R2Y 2F5N 2F5O 2F5P 2F5Q
• Descriptor: 5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*TP*CP*GP*GP*AP*CP*GP*C)-3', 5'-D(*TP*GP*C*GP*TP*CP*CP*(8OG)P*AP*GP*TP*CP*TP*AP*CP*C)-3', formamidopyrimidine-DNA glycosidase, ... (5 entities in total)
• Functional Keywords: disulfide crosslink, dna glycosylase, dna repair, damage search, control complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Geobacillus stearothermophilus; More
• Total number of polymer chains: 3
• Total formula weight: 40593.30

Authors

Banerjee, A.,Santos, W.L.,Verdine, G.L. (deposition date: 2005-11-26, release date: 2006-03-07, Last modification date: 2023-08-23)

Primary citation

Banerjee, A.,Santos, W.L.,Verdine, G.L.
Structure of a DNA glycosylase searching for lesions.
Science, 311:1153-1157, 2006

PubMed Abstract: DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix while searching for damage.

PubMed: 16497933
DOI: 10.1126/science.1120288

Experimental method

X-RAY DIFFRACTION (2.35 Å)