9enq: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 9enq is ~~ON HOLD until Paper Publication~~

==HSV-1 DNA polymerase-processivity factor complex in exonuclease state active site with 1-bp DNA mismatch==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[9enq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_KOS Human alphaherpesvirus 1 strain KOS] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ENQ OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=9ENQ FirstGlance].

~~Description~~:

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.12Å</td></tr>

[[Category: ~~Unreleased~~ Structures]]

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AS:2-DEOXY-ADENOSINE+-5-THIO-MONOPHOSPHATE'>AS</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[https://proteopedia.org/fgij/fg.htm?mol=9enq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9enq OCA], [https://pdbe.org/9enq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9enq RCSB], [https://www.ebi.ac.uk/pdbsum/9enq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9enq ProSAT]</td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/DPOL_HHV11 DPOL_HHV11] Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication.<ref>PMID:2553735</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Human alphaherpesvirus 1 strain KOS]]

[[Category: Large Structures]]

[[Category: Synthetic construct]]

[[Category: Elias P]]

[[Category: Grunewald K]]

[[Category: Gustavsson E]]

[[Category: Hallberg BM]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9enq is ON HOLD  until Paper Publication
+==HSV-1 DNA polymerase-processivity factor complex in exonuclease state active site with 1-bp DNA mismatch==
+<StructureSection load='9enq' size='340' side='right'caption='[[9enq]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9enq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_KOS Human alphaherpesvirus 1 strain KOS] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ENQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ENQ FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.12&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AS:2-DEOXY-ADENOSINE+-5-THIO-MONOPHOSPHATE'>AS</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=9enq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9enq OCA], [https://pdbe.org/9enq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9enq RCSB], [https://www.ebi.ac.uk/pdbsum/9enq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9enq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DPOL_HHV11 DPOL_HHV11] Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5' to 3' direction. Therefore, it can catalyze the excision of the RNA primers that initiate the synthesis of Okazaki fragments at a replication fork during viral DNA replication.<ref>PMID:2553735</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Human alphaherpesvirus 1 strain KOS]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Elias P]]
+[[Category: Grunewald K]]
+[[Category: Gustavsson E]]
+[[Category: Hallberg BM]]