4idh

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4idh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4idh OCA], [https://pdbe.org/4idh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4idh RCSB], [https://www.ebi.ac.uk/pdbsum/4idh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4idh ProSAT]</span></td></tr>

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== 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<ref>PMID:23630261</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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