7squ: Difference between revisions
New page: '''Unreleased structure''' The entry 7squ is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Goslar chimallin C4 tetramer localized reconstruction== | |||
<StructureSection load='7squ' size='340' side='right'caption='[[7squ]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7squ]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_vB_EcoM_Goslar Escherichia phage vB_EcoM_Goslar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SQU 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]] 2.6Å</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=7squ FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7squ OCA], [https://pdbe.org/7squ PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7squ RCSB], [https://www.ebi.ac.uk/pdbsum/7squ PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7squ ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CHMA_BPGOS CHMA_BPGOS] Self-assembles to forms a proteinaceous shell that encloses the viral DNA and compartmentalizes proteins and DNA during viral infection (Probable). This micrometer-scale compartment contains narrow pores and is the site of viral replication, with the proteins involved in DNA replication localized inside (By similarity). Provides a surface for docking of capsids during packaging (By similarity). Probably protects the viral genome against host defenses (Probable).[UniProtKB:B3FIW8]<ref>PMID:35922510</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR-Cas systems(1). In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors(2-4). However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation. | |||
Architecture and self-assembly of the jumbo bacteriophage nuclear shell.,Laughlin TG, Deep A, Prichard AM, Seitz C, Gu Y, Enustun E, Suslov S, Khanna K, Birkholz EA, Armbruster E, McCammon JA, Amaro RE, Pogliano J, Corbett KD, Villa E Nature. 2022 Aug;608(7922):429-435. doi: 10.1038/s41586-022-05013-4. Epub 2022 , Aug 3. PMID:35922510<ref>PMID:35922510</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7squ" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia phage vB_EcoM_Goslar]] | |||
[[Category: Large Structures]] | |||
[[Category: Amaro RE]] | |||
[[Category: Birkholz EA]] | |||
[[Category: Corbett KD]] | |||
[[Category: Deep A]] | |||
[[Category: Enustun E]] | |||
[[Category: Gu Y]] | |||
[[Category: Khanna K]] | |||
[[Category: Laughlin TG]] | |||
[[Category: Pogliano J]] | |||
[[Category: Prichard AM]] | |||
[[Category: Seitz C]] | |||
[[Category: Suslov S]] | |||
[[Category: Villa E]] | |||
Latest revision as of 08:52, 5 June 2024
Goslar chimallin C4 tetramer localized reconstructionGoslar chimallin C4 tetramer localized reconstruction
Structural highlights
FunctionCHMA_BPGOS Self-assembles to forms a proteinaceous shell that encloses the viral DNA and compartmentalizes proteins and DNA during viral infection (Probable). This micrometer-scale compartment contains narrow pores and is the site of viral replication, with the proteins involved in DNA replication localized inside (By similarity). Provides a surface for docking of capsids during packaging (By similarity). Probably protects the viral genome against host defenses (Probable).[UniProtKB:B3FIW8][1] Publication Abstract from PubMedBacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction-modification and CRISPR-Cas systems(1). In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors(2-4). However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation. Architecture and self-assembly of the jumbo bacteriophage nuclear shell.,Laughlin TG, Deep A, Prichard AM, Seitz C, Gu Y, Enustun E, Suslov S, Khanna K, Birkholz EA, Armbruster E, McCammon JA, Amaro RE, Pogliano J, Corbett KD, Villa E Nature. 2022 Aug;608(7922):429-435. doi: 10.1038/s41586-022-05013-4. Epub 2022 , Aug 3. PMID:35922510[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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