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| | <SX load='5muu' size='340' side='right' viewer='molstar' caption='[[5muu]], [[Resolution|resolution]] 4.00Å' scene=''> | | <SX load='5muu' size='340' side='right' viewer='molstar' caption='[[5muu]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5muu]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_phi6 Pseudomonas phage phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MUU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MUU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5muu]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUU FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-triphosphatase Nucleoside-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.15 3.6.1.15] </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]] 4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5muu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muu OCA], [http://pdbe.org/5muu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5muu RCSB], [http://www.ebi.ac.uk/pdbsum/5muu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5muu ProSAT]</span></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=5muu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muu OCA], [https://pdbe.org/5muu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5muu RCSB], [https://www.ebi.ac.uk/pdbsum/5muu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5muu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P1_BPPH6 P1_BPPH6]] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging. [[http://www.uniprot.org/uniprot/CAPSD_BPPH6 CAPSD_BPPH6]] Assembles to form an icosahedral capsid with a T=13 symmetry. Drives the penetration of the inner capsid (core) into the cytoplasm.<ref>PMID:10545509</ref> <ref>PMID:17292834</ref> [[http://www.uniprot.org/uniprot/P4_BPPH6 P4_BPPH6]] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.<ref>PMID:12239286</ref> | + | [https://www.uniprot.org/uniprot/P1_BPPH6 P1_BPPH6] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nucleoside-triphosphatase]] | + | [[Category: Pseudomonas virus phi6]] |
| - | [[Category: Pseudomonas phage phi6]] | + | [[Category: El Omari K]] |
| - | [[Category: Huiskonen, J T]] | + | [[Category: Huiskonen JT]] |
| - | [[Category: Ilca, S L]] | + | [[Category: Ilca SL]] |
| - | [[Category: Kotecha, A]] | + | [[Category: Kotecha A]] |
| - | [[Category: Omari, K El]]
| + | [[Category: Poranen MM]] |
| - | [[Category: Poranen, M M]] | + | [[Category: Stuart DI]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Sun X]] |
| - | [[Category: Sun, X]] | + | [[Category: Sun Z]] |
| - | [[Category: Sun, Z]] | + | |
| - | [[Category: Icosahedral virus capsid shell]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
P1_BPPH6 P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging.
Publication Abstract from PubMed
Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage phi6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the phi6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution.
Double-stranded RNA virus outer shell assembly by bona fide domain-swapping.,Sun Z, El Omari K, Sun X, Ilca SL, Kotecha A, Stuart DI, Poranen MM, Huiskonen JT Nat Commun. 2017 Mar 13;8:14814. doi: 10.1038/ncomms14814. PMID:28287099[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun Z, El Omari K, Sun X, Ilca SL, Kotecha A, Stuart DI, Poranen MM, Huiskonen JT. Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. Nat Commun. 2017 Mar 13;8:14814. doi: 10.1038/ncomms14814. PMID:28287099 doi:http://dx.doi.org/10.1038/ncomms14814
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