1UDI

NUCLEOTIDE MIMICRY IN THE CRYSTAL STRUCTURE OF THE URACIL-DNA GLYCOSYLASE-URACIL GLYCOSYLASE INHIBITOR PROTEIN COMPLEX

Summary for 1UDI

• Entry DOI: 10.2210/pdb1udi/pdb
• Descriptor: URACIL-DNA GLYCOSYLASE, URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN (3 entities in total)
• Functional Keywords: hydrolase-inhibitor complex, hydrolase/inhibitor
• Biological source: Herpes simplex virus (type 1 / strain 17); More
• Total number of polymer chains: 2
• Total formula weight: 36717.93

Authors

Pearl, L.H.,Savva, R. (deposition date: 1995-10-30, release date: 1996-03-08, Last modification date: 2024-02-14)

Primary citation

Savva, R.,Pearl, L.H.
Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex.
Nat.Struct.Biol., 2:752-757, 1995

PubMed Abstract: The Bacillus subtilis bacteriophages PBS-1 and PBS-2 protect their uracil-containing DNA by expressing an inhibitor protein (UGI) which inactivates the host uracil-DNA glycosylase (UDGase) base-excision repair enzyme. Also, PBS1/2 UGI efficiently inactivates UDGases from other biological sources, including the enzyme from herpes simplex virus type-1 (HSV-1). The crystal structure of the HSV-1 UDGase-PBS1 UGI complex at 2.7 angstrum reveals an alpha-beta-alpha sandwich structure for UGI which interacts with conserved regions of UDGase involved in DNA binding, and directly mimics protein-DNA interactions observed in the UDGase-oligonucleotide complex. The inhibitor completely blocks access to the active site of UDGase, but makes no direct contact with the uracil-binding pocket itself.

PubMed: 7552746
DOI: 10.1038/nsb0995-752

Experimental method

X-RAY DIFFRACTION (2.7 Å)