4QCB

Protein-DNA complex of Vaccinia virus D4 with double-stranded non-specific DNA

Summary for 4QCB

• Entry DOI: 10.2210/pdb4qcb/pdb
• Related: 4DOF 4DOG 4LZB 4QC9 4QCA
• Descriptor: Uracil-DNA glycosylase, 5'-D(*GP*CP*AP*AP*AP*CP*GP*TP*TP*TP*GP*C)-3', GLYCEROL, ... (4 entities in total)
• Functional Keywords: dna repair enzyme, component of processivity factor, a20, poxvirus, hydrolase-dna complex, hydrolase/dna
• Biological source: Vaccinia virus (VACV)
• Total number of polymer chains: 4
• Total formula weight: 58421.24

Authors

Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D. (deposition date: 2014-05-09, release date: 2015-06-10, Last modification date: 2023-09-20)

Primary citation

Schormann, N.,Banerjee, S.,Ricciardi, R.,Chattopadhyay, D.
Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.
BMC Struct. Biol., 15:10-10, 2015

PubMed Abstract: Uracil-DNA glycosylases are evolutionarily conserved DNA repair enzymes. However, vaccinia virus uracil-DNA glycosylase (known as D4), also serves as an intrinsic and essential component of the processive DNA polymerase complex during DNA replication. In this complex D4 binds to a unique poxvirus specific protein A20 which tethers it to the DNA polymerase. At the replication fork the DNA scanning and repair function of D4 is coupled with DNA replication. So far, DNA-binding to D4 has not been structurally characterized.

PubMed: 26031450
DOI: 10.1186/s12900-015-0037-1

Experimental method

X-RAY DIFFRACTION (2.89 Å)