7sqr

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<StructureSection load='7sqr' size='340' side='right'caption='[[7sqr]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='7sqr' size='340' side='right'caption='[[7sqr]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7sqr]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SQR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7sqr]] is a 12 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=7SQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SQR FirstGlance]. <br>
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</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=7sqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sqr OCA], [https://pdbe.org/7sqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sqr RCSB], [https://www.ebi.ac.uk/pdbsum/7sqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sqr ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7sqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sqr OCA], [https://pdbe.org/7sqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sqr RCSB], [https://www.ebi.ac.uk/pdbsum/7sqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sqr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GP105_BP201 GP105_BP201]] Forms a proteinaceous shell that encloses the viral DNA and compartmentalizes proteins and DNA during viral infection (PubMed:28813669, PubMed:28082593). This shell is the site of viral replication, with the proteins involved in DNA replication localized inside the compartment (PubMed:28813669, PubMed:28082593). Provides a surface for docking of capsids during packaging (PubMed:28082593).<ref>PMID:28082593</ref> <ref>PMID:28813669</ref>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== 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.
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.
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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>
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Amaro, R E]]
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[[Category: Pseudomonas phage 201phi2-1]]
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[[Category: Birkholz, E A]]
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[[Category: Amaro RE]]
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[[Category: Corbett, K D]]
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[[Category: Birkholz EA]]
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[[Category: Deep, A]]
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[[Category: Corbett KD]]
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[[Category: Enustun, E]]
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[[Category: Deep A]]
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[[Category: Gu, Y]]
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[[Category: Enustun E]]
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[[Category: Khanna, K]]
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[[Category: Gu Y]]
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[[Category: Laughlin, T G]]
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[[Category: Khanna K]]
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[[Category: Pogliano, J]]
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[[Category: Laughlin TG]]
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[[Category: Prichard, A M]]
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[[Category: Pogliano J]]
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[[Category: Seitz, C]]
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[[Category: Prichard AM]]
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[[Category: Suslov, S]]
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[[Category: Seitz C]]
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[[Category: Villa, E]]
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[[Category: Suslov S]]
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[[Category: Phage]]
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[[Category: Villa E]]
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[[Category: Structural protein]]
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[[Category: Viral protein]]
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Current revision

201phi2-1 Chimallin localized tetramer reconstruction

PDB ID 7sqr

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