8igg
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8igg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_201phi2-1 Pseudomonas phage 201phi2-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IGG FirstGlance]. <br> | <table><tr><td colspan='2'>[[8igg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_201phi2-1 Pseudomonas phage 201phi2-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IGG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IGG FirstGlance]. <br> | ||
| - | </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=8igg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8igg OCA], [https://pdbe.org/8igg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8igg RCSB], [https://www.ebi.ac.uk/pdbsum/8igg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8igg ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.09Å</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=8igg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8igg OCA], [https://pdbe.org/8igg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8igg RCSB], [https://www.ebi.ac.uk/pdbsum/8igg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8igg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CHMA_BP201 CHMA_BP201] Self-assembles to forms a proteinaceous shell that encloses the viral DNA and compartmentalizes proteins and DNA during viral infection (PubMed:28082593, PubMed:28813669, PubMed:35922510). This micrometer-scale compartment contains narrow pores and is the site of viral replication, with the proteins involved in DNA replication localized inside (PubMed:28082593, PubMed:28813669, PubMed:35922510). Provides a surface for docking of capsids during packaging (PubMed:28082593, PubMed:28813669). Probably protects the viral genome against host defenses (Probable).<ref>PMID:28082593</ref> <ref>PMID:28813669</ref> <ref>PMID:35922510</ref> <ref>PMID:35922510</ref> | [https://www.uniprot.org/uniprot/CHMA_BP201 CHMA_BP201] Self-assembles to forms a proteinaceous shell that encloses the viral DNA and compartmentalizes proteins and DNA during viral infection (PubMed:28082593, PubMed:28813669, PubMed:35922510). This micrometer-scale compartment contains narrow pores and is the site of viral replication, with the proteins involved in DNA replication localized inside (PubMed:28082593, PubMed:28813669, PubMed:35922510). Provides a surface for docking of capsids during packaging (PubMed:28082593, PubMed:28813669). Probably protects the viral genome against host defenses (Probable).<ref>PMID:28082593</ref> <ref>PMID:28813669</ref> <ref>PMID:35922510</ref> <ref>PMID:35922510</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The jumbo phages encode proteins that assemble to form a nucleus-like compartment in infected cells. Here we report the cryo-EM structure and biochemistry characterization of gp105, a protein that is encoded by the jumbo phage 201phi2-1 and is involved in the formation of the nucleus-like compartment in phage 201phi2-1 infected Pseudomonas chlororaphis. We found that, although most gp105 molecules are in the monomeric state in solution, a small portion of gp105 assemble to form large sheet-like assemblies and small cube-like particles. Reconstruction of the cube-like particles showed that the particle consists of six flat head-to-tail tetramers arranged into an octahedral cube. The four molecules at the contact interface of two head-to-tail tetramers are 2-fold symmetry-related and constitute a concave tetramer. Further reconstructions without applying symmetry showed that molecules in the particles around the distal ends of a 3-fold axis are highly dynamic and have the tendency to open up the assembly. Local classifications and refinements of the concave tetramers in the cube-like particle resulted in a map of the concave tetramer at a resolution of 4.09 A. Structural analysis of the concave tetramer indicates that the N and C terminal fragments of gp105 are important for mediating the intermolecular interactions, which was further confirmed by mutagenesis studies. Biochemistry assays showed that, in solution, the cube-like particles of gp105 are liable to either disassemble to form the monomers or recruit more molecules to form the high molecular weight lattice-like assembly. We also found that monomeric gp105s can self-assemble to form large sheet-like assemblies in vitro, and the assembly of gp105 in vitro is a reversible dynamic process and temperature-dependent. Taken together, our results revealed the dynamic assembly of gp105, which helps to understand the development and function of the nucleus-like compartment assembled by phage-encoded proteins. | ||
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| + | Structural studies of the nucleus-like assembly of jumbo bacteriophage 201phi2-1.,Liu Z, Xiang Y Front Microbiol. 2023 Apr 17;14:1170112. doi: 10.3389/fmicb.2023.1170112. , eCollection 2023. PMID:37138628<ref>PMID:37138628</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8igg" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
C2 reconstruction of the concave tetramer in the cube-like assembly of 201Phi2-1 gp105
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