4zni: Difference between revisions

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-'''Unreleased structure'''
-The entry 4zni is ON HOLD  until Paper Publication
+==Thermus Phage P74-26 Large Terminase ATPase domain (I 2 3 space group)==
+<StructureSection load='4zni' size='340' side='right'caption='[[4zni]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4zni]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P74-26 Thermus virus P74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZNI 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]] 2.097&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4zni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zni OCA], [https://pdbe.org/4zni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zni RCSB], [https://www.ebi.ac.uk/pdbsum/4zni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zni ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A7XXR1_BP742 A7XXR1_BP742] The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. 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 packaged with the DNA, the terminase complex is substituted by the tail.[HAMAP-Rule:MF_04146]
-Authors: Hilbert, B.J., Hayes, J.A., Stone, N.P., Duffy, C.M., Sankaran, B., Kelch, B.A.
+==See Also==
+*[[Terminase 3D Structures|Terminase 3D Structures]]
-Description:
+__TOC__
-[[Category: Unreleased Structures]]
+</StructureSection>
-[[Category: Sankaran, B]]
+[[Category: Large Structures]]
-[[Category: Kelch, B.A]]
+[[Category: Thermus virus P74-26]]
-[[Category: Hilbert, B.J]]
+[[Category: Duffy CM]]
-[[Category: Stone, N.P]]
+[[Category: Hayes JA]]
-[[Category: Hayes, J.A]]
+[[Category: Hilbert BJ]]
-[[Category: Duffy, C.M]]
+[[Category: Kelch BA]]
+[[Category: Sankaran B]]
+[[Category: Stone NP]]