9i86
From Proteopedia
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m (Protected "9i86" [edit=sysop:move=sysop]) |
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- | '''Unreleased structure''' | ||
- | + | ==Enterobacteriaphage PRD1 - P12 protein filament in complex with poly(dT) ssDNA== | |
+ | <StructureSection load='9i86' size='340' side='right'caption='[[9i86]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[9i86]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_PRD1 Enterobacteria phage PRD1] 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=9I86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I86 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]] 2.75Å</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=9i86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i86 OCA], [https://pdbe.org/9i86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i86 RCSB], [https://www.ebi.ac.uk/pdbsum/9i86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i86 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/VP12_BPPRD VP12_BPPRD] Binds to single-stranded DNA (ssDNA). Has a regulatory effect on phage DNA metabolism and transcription of early genes. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Protein-primed DNA replication is a unique mechanism, bioorthogonal to other known DNA replication modes. It relies on specialised single-stranded DNA (ssDNA)-binding proteins (SSBs) to stabilise ssDNA intermediates by unknown mechanisms. Here, we present the structural and biochemical characterisation of P12, an SSB from bacteriophage PRD1. High-resolution cryo-electron microscopy reveals that P12 forms a unique, cooperative filament along ssDNA. Each protomer binds the phosphate backbone of 6 nucleotides in a sequence-independent manner, protecting ssDNA from nuclease degradation. Filament formation is driven by an intrinsically disordered C-terminal tail, facilitating cooperative binding. We identify residues essential for ssDNA interaction and link the ssDNA-binding ability of P12 to toxicity in host cells. Bioinformatic analyses place the P12 fold as a distinct branch within the OB-like fold family. This work offers new insights into protein-primed DNA replication and lays a foundation for biotechnological applications. | ||
- | + | Structural basis for cooperative ssDNA binding by bacteriophage protein filament P12.,Trager LK, Degen M, Pereira J, Durairaj J, Teixeira RD, Hiller S, Huguenin-Dezot N Nucleic Acids Res. 2025 Feb 27;53(5):gkaf132. doi: 10.1093/nar/gkaf132. PMID:40052821<ref>PMID:40052821</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 9i86" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Enterobacteria phage PRD1]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Degen M]] | ||
+ | [[Category: Hiller S]] | ||
+ | [[Category: Traeger KL]] |
Current revision
Enterobacteriaphage PRD1 - P12 protein filament in complex with poly(dT) ssDNA
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