4C2U
Crystal structure of Deinococcus radiodurans UvrD in complex with DNA, Form 1
Summary for 4C2U
| Entry DOI | 10.2210/pdb4c2u/pdb |
| Related | 4C2T |
| Descriptor | DNA HELICASE II, REV25, FOR25, ... (9 entities in total) |
| Functional Keywords | hydrolase-dna complex, dna repair, dna helicases, nucleotide excision repair, hydrolase/dna |
| Biological source | DEINOCOCCUS RADIODURANS More |
| Total number of polymer chains | 4 |
| Total formula weight | 165033.99 |
| Authors | Stelter, M.,Acajjaoui, S.,McSweeney, S.,Timmins, J. (deposition date: 2013-08-20, release date: 2013-10-30, Last modification date: 2023-12-20) |
| Primary citation | Stelter, M.,Acajjaoui, S.,Mcsweeney, S.,Timmins, J. Structural and Mechanistic Insight Into DNA Unwinding by Deinococcus Radiodurans Uvrd. Plos One, 8:77364-, 2013 Cited by PubMed Abstract: DNA helicases are responsible for unwinding the duplex DNA, a key step in many biological processes. UvrD is a DNA helicase involved in several DNA repair pathways. We report here crystal structures of Deinococcus radiodurans UvrD (drUvrD) in complex with DNA in different nucleotide-free and bound states. These structures provide us with three distinct snapshots of drUvrD in action and for the first time trap a DNA helicase undergoing a large-scale spiral movement around duplexed DNA. Our structural data also improve our understanding of the molecular mechanisms that regulate DNA unwinding by Superfamily 1A (SF1A) helicases. Our biochemical data reveal that drUvrD is a DNA-stimulated ATPase, can translocate along ssDNA in the 3'-5' direction and shows ATP-dependent 3'-5', and surprisingly also, 5'-3' helicase activity. Interestingly, we find that these translocase and helicase activities of drUvrD are modulated by the ssDNA binding protein. Analysis of drUvrD mutants indicate that the conserved β-hairpin structure of drUvrD that functions as a separation pin is critical for both drUvrD's 3'-5' and 5'-3' helicase activities, whereas the GIG motif of drUvrD involved in binding to the DNA duplex is essential for the 5'-3' helicase activity only. These special features of drUvrD may reflect its involvement in a wide range of DNA repair processes in vivo. PubMed: 24143224DOI: 10.1371/JOURNAL.PONE.0077364 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
Download full validation report
