9ut7: Difference between revisions
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The | ==The Primase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir== | ||
<StructureSection load='9ut7' size='340' side='right'caption='[[9ut7]], [[Resolution|resolution]] 3.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9ut7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UT7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.08Å</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ut7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ut7 OCA], [https://pdbe.org/9ut7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ut7 RCSB], [https://www.ebi.ac.uk/pdbsum/9ut7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ut7 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRIM_HHV11 PRIM_HHV11] Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.[HAMAP-Rule:MF_04011]<ref>PMID:7775476</ref> <ref>PMID:8189507</ref> [https://www.uniprot.org/uniprot/SUMO_YEAST SUMO_YEAST] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer (PubMed:9312010). Sumoylation, the attachment of SUMO to target proteins, regulates multiple cellular events (By similarity).[UniProtKB:O13351]<ref>PMID:9312010</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human alphaherpesvirus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Hamada K]] | |||
[[Category: Kise Y]] | |||
[[Category: Nureki O]] | |||
[[Category: Sato K]] | |||
[[Category: Sengoku T]] | |||
Latest revision as of 06:32, 8 April 2026
The Primase module of the helicase-primase complex from HHV1 bound with ssDNA and pritelivir
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