3p9a
From Proteopedia
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| - | [[ | + | ==An atomic view of the nonameric small terminase subunit of Bacteriophage P22== |
| + | <StructureSection load='3p9a' size='340' side='right' caption='[[3p9a]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3p9a]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P9A FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 Enterobacteria phage P22])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3p9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p9a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p9a RCSB], [http://www.ebi.ac.uk/pdbsum/3p9a PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Packaging of viral genomes into empty procapsids is powered by a large DNA-packaging motor. In most viruses, this machine is composed of a large (L) and a small (S) terminase subunit complexed with a dodecamer of portal protein. Here we describe the 1.75 A crystal structure of the bacteriophage P22 S-terminase in a nonameric conformation. The structure presents a central channel approximately 23 A in diameter, sufficiently large to accommodate hydrated B-DNA. The last 23 residues of S-terminase are essential for binding to DNA and assembly to L-terminase. Upon binding to its own DNA, S-terminase functions as a specific activator of L-terminase ATPase activity. The DNA-dependent stimulation of ATPase activity thus rationalizes the exclusive specificity of genome-packaging motors for viral DNA in the crowd of host DNA, ensuring fidelity of packaging and avoiding wasteful ATP hydrolysis. This posits a model for DNA-dependent activation of genome-packaging motors of general interest in virology. | ||
| - | + | Small Terminase Couples Viral DNA Binding to Genome-Packaging ATPase Activity.,Roy A, Bhardwaj A, Datta P, Lander GC, Cingolani G Structure. 2012 Jul 3. PMID:22771211<ref>PMID:22771211</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Enterobacteria phage p22]] | [[Category: Enterobacteria phage p22]] | ||
[[Category: Bhardwaj, A.]] | [[Category: Bhardwaj, A.]] | ||
Revision as of 05:25, 4 June 2014
An atomic view of the nonameric small terminase subunit of Bacteriophage P22
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