Structural analysis of point mutations at the Vaccinia virus A20/D4 interface

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 processiv...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2016-09, Vol.72 (9), p.687-691
Hauptverfasser:	Contesto-Richefeu, Céline, Tarbouriech, Nicolas, Brazzolotto, Xavier, Burmeister, Wim P., Peyrefitte, Christophe N., Iseni, Frédéric
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Amino acids Atomic structure Biochemistry, Molecular Biology Catalytic Domain cation-π interaction Cations Cloning, Molecular Crystal structure Crystallization Crystallography, X-Ray Deoxyribonucleic acid DNA DNA polymerase DNA replication DNA-Directed DNA Polymerase DNA-Directed DNA Polymerase - chemistry DNA-Directed DNA Polymerase - genetics DNA-Directed DNA Polymerase - metabolism Enzymatic activity Forming Gene Expression Life Sciences Models, Molecular Plasmids Plasmids - chemistry Plasmids - metabolism Point Mutation Protein Conformation Protein Multimerization protein-protein interface Recombinant Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Research Communications Residues Solvation Structural analysis Structural Biology Uracil-DNA Glycosidase Uracil-DNA Glycosidase - chemistry Uracil-DNA Glycosidase - genetics Uracil-DNA Glycosidase - metabolism Vaccinia virus Vaccinia virus - chemistry Vaccinia virus - metabolism Viral Proteins Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Viruses X-Ray Diffraction X-ray structure
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