3p9a

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==An atomic view of the nonameric small terminase subunit of Bacteriophage P22==
==An atomic view of the nonameric small terminase subunit of Bacteriophage P22==
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<StructureSection load='3p9a' size='340' side='right' caption='[[3p9a]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='3p9a' size='340' side='right'caption='[[3p9a]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3p9a]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. 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>
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<table><tr><td colspan='2'>[[3p9a]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus 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 [https://proteopedia.org/fgij/fg.htm?mol=3P9A FirstGlance]. <br>
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</td></tr><tr id='gene'><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 BPP22])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.755&#8491;</td></tr>
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<tr id='resources'><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://pdbe.org/3p9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p9a RCSB], [http://www.ebi.ac.uk/pdbsum/3p9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p9a ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p9a OCA], [https://pdbe.org/3p9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p9a RCSB], [https://www.ebi.ac.uk/pdbsum/3p9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p9a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TERM_BPP22 TERM_BPP22]] Involved in the phage DNA-packaging initiation process. Packaging of DNA occurs by cutting headful-sized fragments in a sequential manner from a DNA concatemer. To initiate this process, protein gp3 recognizes a signal sequence: the pac site.
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[https://www.uniprot.org/uniprot/TERS_BPP22 TERS_BPP22] The terminase small subunit binds to the packaging initiation site and regulates the ATPase activity of the terminase large subunit. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins.<ref>PMID:18775728</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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==See Also==
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*[[Terminase 3D Structures|Terminase 3D Structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3p9a" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpp22]]
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[[Category: Large Structures]]
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[[Category: Bhardwaj, A]]
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[[Category: Salmonella virus P22]]
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[[Category: Cingolani, G]]
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[[Category: Bhardwaj A]]
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[[Category: Roy, A]]
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[[Category: Cingolani G]]
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[[Category: Bacteriophage p22]]
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[[Category: Roy A]]
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[[Category: Dna binding protein]]
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[[Category: Dna packaging]]
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[[Category: Terminase small subunit]]
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Current revision

An atomic view of the nonameric small terminase subunit of Bacteriophage P22

PDB ID 3p9a

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