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5muu

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Revision as of 21:07, 10 April 2020

dsRNA bacteriophage phi6 nucleocapsid

5muu, resolution 4.00Å

Structural highlights

5muu is a 13 chain structure with sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Nucleoside-triphosphatase, with EC number 3.6.1.15
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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. [CAPSD_BPPH6] Assembles to form an icosahedral capsid with a T=13 symmetry. Drives the penetration of the inner capsid (core) into the cytoplasm.^[1] ^[2] [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.^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Poranen MM, Daugelavicius R, Ojala PM, Hess MW, Bamford DH. A novel virus-host cell membrane interaction. Membrane voltage-dependent endocytic-like entry of bacteriophage straight phi6 nucleocapsid. J Cell Biol. 1999 Nov 1;147(3):671-82. PMID:10545509
↑ Jaalinoja HT, Huiskonen JT, Butcher SJ. Electron cryomicroscopy comparison of the architectures of the enveloped bacteriophages phi6 and phi8. Structure. 2007 Feb;15(2):157-67. PMID:17292834 doi:http://dx.doi.org/S0969-2126(07)00026-3
↑ Pirttimaa MJ, Paatero AO, Frilander MJ, Bamford DH. Nonspecific nucleoside triphosphatase P4 of double-stranded RNA bacteriophage phi6 is required for single-stranded RNA packaging and transcription. J Virol. 2002 Oct;76(20):10122-7. PMID:12239286
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5muu"

@@ Line 3: / Line 3: @@
 <SX load='5muu' size='340' side='right' viewer='molstar' caption='[[5muu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
 == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MUU FirstGlance]. <br>
+<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>
 </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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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'>[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>
 </table>
 == Function ==

5muu

From Proteopedia

Revision as of 21:07, 10 April 2020

dsRNA bacteriophage phi6 nucleocapsid

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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