2OWQ

Crystal structure of vaccinia virus uracil-DNA glycosylase

Summary for 2OWQ

• Entry DOI: 10.2210/pdb2owq/pdb
• Related: 1AKZ 2EUG 2OWR
• Descriptor: Uracil-DNA glycosylase, CHLORIDE ION, IMIDAZOLE, ... (6 entities in total)
• Functional Keywords: uracil-dna glycosylase fold in the core: 3 layers (a/b/a), and parallel beta-sheet of 4 strands in the order 2134; novel features: beta-sheets at n- and c-terminus, hydrolase
• Biological source: Vaccinia virus Western Reserve
• Total number of polymer chains: 2
• Total formula weight: 55213.38

Authors

Schormann, N.,Chattopadhyay, D. (deposition date: 2007-02-16, release date: 2007-07-24, Last modification date: 2024-02-21)

Primary citation

Schormann, N.,Grigorian, A.,Samal, A.,Krishnan, R.,DeLucas, L.,Chattopadhyay, D.
Crystal structure of vaccinia virus uracil-DNA glycosylase reveals dimeric assembly
Bmc Struct.Biol., 7:45-45, 2007

PubMed Abstract: Uracil-DNA glycosylases (UDGs) catalyze excision of uracil from DNA. Vaccinia virus, which is the prototype of poxviruses, encodes a UDG (vvUDG) that is significantly different from the UDGs of other organisms in primary, secondary and tertiary structure and characteristic motifs. It adopted a novel catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG:A20 association is essential for assembling of the processive DNA polymerase complex. The structure of the protein must have provisions for such interactions with A20. This paper provides the first glimpse into the structure of a poxvirus UDG.

PubMed: 17605817
DOI: 10.1186/1472-6807-7-45

Experimental method

X-RAY DIFFRACTION (2.4 Å)