4QCA
Crystal structure of Vaccinia virus uracil-DNA glycosylase mutant R167AD4
Summary for 4QCA
| Entry DOI | 10.2210/pdb4qca/pdb |
| Related | 4DOF 4DOG 4IRB 4LZB 4QC9 4QCB |
| Descriptor | Uracil-DNA glycosylase, GLYCEROL, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | dna repair enzyme, component of processivity factor, a20, dna, poxvirus, hydrolase |
| Biological source | Vaccinia virus (VACV) |
| Total number of polymer chains | 4 |
| Total formula weight | 101660.94 |
| Authors | Sartmatova, D.,Nash, T.,Schormann, N.,Nuth, M.,Ricciardi, R.,Banerjee, S.,Chattopadhyay, D. (deposition date: 2014-05-09, release date: 2015-05-13, Last modification date: 2023-09-20) |
| Primary citation | Sartmatova, D.,Nash, T.,Schormann, N.,Nuth, M.,Ricciardi, R.,Banerjee, S.,Chattopadhyay, D. Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr.,Sect.F, 69:295-301, 2013 Cited by PubMed Abstract: Amino-acid residues located at a highly flexible area in the uracil DNA glycosylase of Vaccinia virus were mutated. In the crystal structure of wild-type D4 these residues lie at the dimer interface. Specifically, three mutants were generated: (i) residue Arg167 was replaced with an alanine (R167AD4), (ii) residues Glu171, Ser172 and Pro173 were substituted with three glycine residues (3GD4) and (iii) residues Glu171 and Ser172 were deleted (Δ171-172D4). Mutant proteins were expressed, purified and crystallized in order to investigate the effects of these mutations on the structure of the protein. PubMed: 23519808DOI: 10.1107/S1744309113002716 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
