6A27
Crystal structure of PprA W183R mutant form 1
Summary for 6A27
Entry DOI | 10.2210/pdb6a27/pdb |
Descriptor | DNA repair protein PprA, SULFATE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | dna binding protein |
Biological source | Deinococcus radiodurans R1 |
Total number of polymer chains | 2 |
Total formula weight | 61286.35 |
Authors | Adachi, M.,Shibazaki, C.,Shimizu, R.,Arai, S.,Satoh, K.,Narumi, I.,Kuroki, R. (deposition date: 2018-06-09, release date: 2018-12-26, Last modification date: 2023-11-22) |
Primary citation | Adachi, M.,Shimizu, R.,Shibazaki, C.,Satoh, K.,Fujiwara, S.,Arai, S.,Narumi, I.,Kuroki, R. Extended structure of pleiotropic DNA repair-promoting protein PprA from Deinococcus radiodurans. FASEB J., 33:3647-3658, 2019 Cited by PubMed Abstract: Pleiotropic protein promoting DNA repair A (PprA) is a key protein facilitating the extreme radiation resistance of Deinococcus radiodurans. PprA is a unique protein to the genus Deinococcus and exists as an oligomer ranging from a tetramer to an ∼100-mer depending on protein concentrations. Here, the X-ray crystal structure of PprA was determined to clarify how PprA confers radiation resistance. The tertiary structure of dimeric PprA was elucidated by using mutants obtained with random and site-directed mutagenesis methods (W183R and A139R); these mutants have disabled DNA binding and polymerization functions. Because the mutant A139R and W183R proteins have dimeric assemblies with 2 different interfaces (Interfaces 1 and 2), the linear and oligomerized PprA model was constructed as a left-handed face-to-face periodic screw structure. In addition, the linear structure in solution was confirmed by small-angle scattering experiments. The site-directed mutational analysis identified essential basic amino acids for DNA binding. These analytical data support the hypothesis that a complex assembly of PprA molecules, which are extended and have a screw structure, surrounds and stretches the DNA strand, acting as a novel guide to colocalize the DNA strands for efficient DNA repairs.-Adachi, M., Shimizu, R., Shibazaki, C., Satoh, K., Fujiwara, S., Arai, S., Narumi, I., Kuroki, R. Extended structure of pleiotropic DNA repair-promoting protein PprA from Deinococcus radiodurans. PubMed: 30481062DOI: 10.1096/fj.201801506R PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.353 Å) |
Structure validation
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