4iee: Difference between revisions
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== | ==Crystal Structure of the large terminase subunit gp2 of bacterial virus Sf6 complexed with ATP-r-S== | ||
[[4iee]] is a 1 chain structure with sequence from [ | <StructureSection load='4iee' size='340' side='right'caption='[[4iee]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
[[ | == Structural highlights == | ||
[[ | <table><tr><td colspan='2'>[[4iee]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_virus_Sf6 Shigella virus Sf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IEE FirstGlance]. <br> | ||
[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</td></tr> | ||
[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4iee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iee OCA], [https://pdbe.org/4iee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iee RCSB], [https://www.ebi.ac.uk/pdbsum/4iee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iee ProSAT]</span></td></tr> | |||
</table> | |||
[[Category: | == Function == | ||
[[Category: | [https://www.uniprot.org/uniprot/Q716H3_BPSFV Q716H3_BPSFV] | ||
[[Category: | <div style="background-color:#fffaf0;"> | ||
[[Category: | == Publication Abstract from PubMed == | ||
[[Category: | 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. | ||
[[Category: | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4iee" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Terminase 3D Structures|Terminase 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shigella virus Sf6]] | |||
[[Category: Christensen T]] | |||
[[Category: Kamau Y]] | |||
[[Category: Tang L]] | |||
[[Category: Zhao H]] | |||
Latest revision as of 18:21, 20 September 2023
Crystal Structure of the large terminase subunit gp2 of bacterial virus Sf6 complexed with ATP-r-SCrystal Structure of the large terminase subunit gp2 of bacterial virus Sf6 complexed with ATP-r-S
Structural highlights
FunctionPublication Abstract from PubMedMany 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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