Summary for 5ZB6
| Entry DOI | 10.2210/pdb5zb6/pdb |
| NMR Information | BMRB: 16864 |
| Descriptor | UVI31+ (1 entity in total) |
| Functional Keywords | structure from cyana 3.0, plant protein |
| Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
| Total number of polymer chains | 1 |
| Total formula weight | 13328.99 |
| Authors | Rout, A.K.,Patel, S.,Rao, B.J.,Chary, K.V. (deposition date: 2018-02-10, release date: 2018-10-03, Last modification date: 2024-05-15) |
| Primary citation | Rout, A.K.,Singh, H.,Patel, S.,Raghvan, V.,Gautam, S.,Minda, R.,Rao, B.J.,Chary, K.V.R. Structural characterization of a novel KH-domain containing plant chloroplast endonuclease Sci Rep, 8:13750-13750, 2018 Cited by PubMed Abstract: Chlamydomonas reinhardtii is a single celled alga that undergoes apoptosis in response to UV-C irradiation. UVI31+, a novel UV-inducible DNA endonuclease in C. reinhardtii, which normally localizes near cell wall and pyrenoid regions, gets redistributed into punctate foci within the whole chloroplast, away from the pyrenoid, upon UV-stress. Solution NMR structure of the first putative UV inducible endonuclease UVI31+ revealed an α-β-β-α-α-β fold similar to BolA and type II KH-domain ubiquitous protein families. Three α-helices of UVI31+ constitute one side of the protein surface, which are packed to the other side, made of three-stranded β-sheet, with intervening hydrophobic residues. A twenty-three residues long polypeptide stretch (D54-H76) connecting β and β strands is found to be highly flexible. Interestingly, UVI31+ recognizes the DNA primarily through its β-sheet. We propose that the catalytic triad residues involving Ser114, His95 and Thr116 facilitate DNA endonuclease activity of UVI31+. Further, decreased endonuclease activity of the S114A mutant is consistent with the direct participation of Ser114 in the catalysis. This study provides the first structural description of a plant chloroplast endonuclease that is regulated by UV-stress response. PubMed: 30214061DOI: 10.1038/s41598-018-31142-w PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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