Summary information and primary citation

PDB-id
2f5s; SNAP-derived features in text and JSON formats; DNAproDB
Class
hydrolase-DNA
Method
X-ray (2.35 Å)
Summary
Catalytically inactive (e3q) mutm crosslinked to oxog:c containing DNA cc1
Reference
Banerjee A, Santos WL, Verdine GL (2006): "Structure of a DNA glycosylase searching for lesions." Science, 311, 1153-1157. doi: 10.1126/science.1120288.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js