5muw

From Proteopedia

(Difference between revisions)

Current revision

Atomic structure of P4 packaging enzyme fitted into a localized reconstruction of bacteriophage phi6 vertex

5muw, resolution 2.80Å

Structural highlights

5muw is a 6 chain structure with sequence from Pseudomonas virus phi6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.8Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

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^[2]

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

References

↑ 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/5muw"

@@ Line 1: / Line 1: @@
 ==Atomic structure of P4 packaging enzyme fitted into a localized reconstruction of bacteriophage phi6 vertex==
-<StructureSection load='5muw' size='340' side='right' caption='[[5muw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<SX load='5muw' size='340' side='right' viewer='molstar' caption='[[5muw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5muw]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MUW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MUW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5muw]] is a 6 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=5MUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4blo|4blo]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5muw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muw OCA], [https://pdbe.org/5muw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5muw RCSB], [https://www.ebi.ac.uk/pdbsum/5muw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5muw ProSAT]</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=5muw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muw OCA], [http://pdbe.org/5muw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5muw RCSB], [http://www.ebi.ac.uk/pdbsum/5muw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5muw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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/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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Nucleoside-triphosphatase]]
+[[Category: Large Structures]]
-[[Category: Huiskonen, J T]]
+[[Category: Pseudomonas virus phi6]]
-[[Category: Ilca, S]]
+[[Category: El Omari K]]
-[[Category: Kotecha, A]]
+[[Category: Huiskonen JT]]
-[[Category: Omari, K El]]
+[[Category: Ilca S]]
-[[Category: Poranen, M M]]
+[[Category: Kotecha A]]
-[[Category: Stuart, D I]]
+[[Category: Poranen MM]]
-[[Category: Sun, X]]
+[[Category: Stuart DI]]
-[[Category: Sun, Z]]
+[[Category: Sun X]]
-[[Category: Atpase]]
+[[Category: Sun Z]]
-[[Category: Hydrolase]]
-[[Category: Hyrdolase]]
-[[Category: Packaging]]
-[[Category: Vertex]]

5muw

From Proteopedia

Current revision

Atomic structure of P4 packaging enzyme fitted into a localized reconstruction of bacteriophage phi6 vertex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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