Summary information and primary citation

PDB-id
1lwv; SNAP-derived features in text and JSON formats; DNAproDB
Class
hydrolase-DNA
Method
X-ray (2.3 Å)
Summary
Borohydride-trapped hogg1 intermediate structure co-crystallized with 8-aminoguanine
Reference
Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL (2003): "Product-Assisted Catalysis in Base Excision DNA Repair." Nat.Struct.Biol., 10, 204-211. doi: 10.1038/nsb902.
Abstract
Most spontaneous damage to bases in DNA is corrected through the action of the base-excision DNA repair pathway. Base excision repair is initiated by DNA glycosylases, lesion-specific enzymes that intercept aberrant bases in DNA and catalyze their excision. How such proteins accomplish the feat of catalyzing no fewer than five sequential reaction steps using a single active site has been unknown. To help answer this, we report the structure of a trapped catalytic intermediate in DNA repair by human 8-oxoguanine DNA glycosylase. This structure and supporting biochemical results reveal that the enzyme sequesters the excised lesion base and exploits it as a cofactor to participate in catalysis. To our knowledge, the present example represents the first documented case of product-assisted catalysis in an enzyme-catalyzed reaction.

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

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