4ife

Crystal Structure of the large terminase subunit gp2 of bacterial virus Sf6 complexed with ATP

spinqualitylabelsall models 4ife, resolution 3.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ife is a 1 chain structure with sequence from Bpsfv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP Related: 4idh, 4iee, 4iei Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Many DNA viruses use powerful molecular motors to cleave concatemeric viral DNA into genome-length units and package them into preformed procapsid powered by ATP hydrolysis. Here we report the structures of the DNA-packaging motor gp2 of bacteriophage Sf6, which reveal a unique clade of RecA-like ATPase domain and an RNase H-like nuclease domain tethered by a regulatory linker domain, exhibiting a strikingly distinct domain arrangement. The gp2 structures complexed with nucleotides reveal, at the atomic detail, the catalytic center embraced by the ATPase domain and the linker domain. The gp2 nuclease activity is modulated by the ATPase domain and is stimulated by ATP. An extended DNA-binding surface is formed by the linker domain and the nuclease domain. These results suggest a unique mechanism for translation of chemical reaction into physical motion of DNA and provide insights into coordination of DNA translocation and cleavage in a viral DNA-packaging motor, which may be achieved via linker-domain-mediated interdomain communication driven by ATP hydrolysis. Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage.,Zhao H, Christensen TE, Kamau YN, Tang L Proc Natl Acad Sci U S A. 2013 May 14;110(20):8075-8080. Epub 2013 Apr 29. PMID:23630261 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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