5JKS

vaccinia virus D4 R167A mutant /A20(1-50)

Summary for 5JKS

• Entry DOI: 10.2210/pdb5jks/pdb
• Descriptor: Uracil-DNA glycosylase, DNA polymerase processivity factor component A20, SULFATE ION, ... (4 entities in total)
• Functional Keywords: dna polymerase processivity factor, dna binding, dna polymerase binding, hydrolase-replication complex, hydrolase, hydrolase/replication
• Biological source: Vaccinia virus (strain Copenhagen) (VACV); More
• Total number of polymer chains: 4
• Total formula weight: 65478.29

Authors

Contesto-Richefeu, C.,Tarbouriech, N.,Brazzolotto, X.,Burmeister, W.P.,Peyrefitte, C.N.,Iseni, F. (deposition date: 2016-04-26, release date: 2016-09-14, Last modification date: 2024-01-10)

Primary citation

Contesto-Richefeu, C.,Tarbouriech, N.,Brazzolotto, X.,Burmeister, W.P.,Peyrefitte, C.N.,Iseni, F.
Structural analysis of point mutations at the Vaccinia virus A20/D4 interface.
Acta Crystallogr.,Sect.F, 72:687-691, 2016

PubMed Abstract: The Vaccinia virus polymerase holoenzyme is composed of three subunits: E9, the catalytic DNA polymerase subunit; D4, a uracil-DNA glycosylase; and A20, a protein with no known enzymatic activity. The D4/A20 heterodimer is the DNA polymerase cofactor, the function of which is essential for processive DNA synthesis. The recent crystal structure of D4 bound to the first 50 amino acids of A20 (D4/A201-50) revealed the importance of three residues, forming a cation-π interaction at the dimerization interface, for complex formation. These are Arg167 and Pro173 of D4 and Trp43 of A20. Here, the crystal structures of the three mutants D4-R167A/A201-50, D4-P173G/A201-50 and D4/A201-50-W43A are presented. The D4/A20 interface of the three structures has been analysed for atomic solvation parameters and cation-π interactions. This study confirms previous biochemical data and also points out the importance for stability of the restrained conformational space of Pro173. Moreover, these new structures will be useful for the design and rational improvement of known molecules targeting the D4/A20 interface.

PubMed: 27599859
DOI: 10.1107/S2053230X16011778

Experimental method

X-RAY DIFFRACTION (2.79 Å)