6m5r: Difference between revisions
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==== | ==The coordinates of the apo monomeric terminase complex== | ||
<StructureSection load='6m5r' size='340' side='right'caption='[[6m5r]]' scene=''> | <StructureSection load='6m5r' size='340' side='right'caption='[[6m5r]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6m5r]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M5R FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6m5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m5r OCA], [https://pdbe.org/6m5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m5r RCSB], [https://www.ebi.ac.uk/pdbsum/6m5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m5r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRM3_HHV11 TRM3_HHV11] Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterodimerizes with small terminase protein to be docked on capsid portal protein. The latter forms a ring in which genomic DNA in translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation. | |||
==See Also== | |||
*[[Terminase 3D Structures|Terminase 3D Structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human alphaherpesvirus 1 strain 17]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chen ZH]] | ||
[[Category: Rao ZH]] | |||
[[Category: Wang N]] | |||
[[Category: Wang XX]] | |||
[[Category: Yang P]] | |||
[[Category: Yang YX]] | |||
[[Category: Zhou ZH]] | |||
Latest revision as of 13:48, 27 March 2024
The coordinates of the apo monomeric terminase complexThe coordinates of the apo monomeric terminase complex
Structural highlights
FunctionTRM3_HHV11 Component of the molecular motor that translocates genomic DNA in empty capsid during DNA packaging. Heterodimerizes with small terminase protein to be docked on capsid portal protein. The latter forms a ring in which genomic DNA in translocated into the capsid. May have or induce an endonuclease activity to cleave the genome concatemer after encapsidation. See Also |
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