1LAU

URACIL-DNA GLYCOSYLASE

Summary for 1LAU

• Entry DOI: 10.2210/pdb1lau/pdb
• Descriptor: DNA (5'-D(*TP*TP*T)-3'), PROTEIN (URACIL-DNA GLYCOSYLASE (E.C.3.2.2.-)) (3 entities in total)
• Functional Keywords: hydrolase, glycosidase, dna, hydrolase-dna complex, hydrolase/dna
• Biological source: Human herpesvirus 1 (Herpes simplex virus type 1)
• Total number of polymer chains: 2
• Total formula weight: 28234.07

Authors

Pearl, L.H.,Savva, R. (deposition date: 1996-01-03, release date: 1996-06-10, Last modification date: 2024-02-14)

Primary citation

Savva, R.,McAuley-Hecht, K.,Brown, T.,Pearl, L.
The structural basis of specific base-excision repair by uracil-DNA glycosylase.
Nature, 373:487-493, 1995

PubMed Abstract: The 1.75-A crystal structure of the uracil-DNA glycosylase from herpes simplex virus type-1 reveals a new fold, distantly related to dinucleotide-binding proteins. Complexes with a trideoxynucleotide, and with uracil, define the DNA-binding site and allow a detailed understanding of the exquisitely specific recognition of uracil in DNA. The overall structure suggests binding models for elongated single- and double-stranded DNA substrates. Conserved residues close to the uracil-binding site suggest a catalytic mechanism for hydrolytic base excision.

PubMed: 7845459
DOI: 10.1038/373487a0

Experimental method

X-RAY DIFFRACTION (1.8 Å)