4c2t

Crystal structure of full length Deinococcus radiodurans UvrD in complex with DNA

spinqualitylabelsall models 4c2t, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c2t is a 8 chain structure with sequence from "micrococcus_radiodurans"_raj_et_al._1960 "micrococcus radiodurans" raj et al. 1960. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, MG Related: 4c2u Activity: DNA helicase, with EC number 3.6.4.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-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. Structural and Mechanistic Insight into DNA Unwinding by Deinococcus radiodurans UvrD.,Stelter M, Acajjaoui S, McSweeney S, Timmins J PLoS One. 2013 Oct 15;8(10):e77364. doi: 10.1371/journal.pone.0077364. PMID:24143224 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase

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