3cnf

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Current revision (09:37, 21 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cnf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CNF FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cnf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori_cypovirus_1 Bombyx mori cypovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CNF 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=3cnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cnf OCA], [https://pdbe.org/3cnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cnf RCSB], [https://www.ebi.ac.uk/pdbsum/3cnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cnf 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]] 3.88&#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=3cnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cnf OCA], [https://pdbe.org/3cnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cnf RCSB], [https://www.ebi.ac.uk/pdbsum/3cnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cnf ProSAT]</span></td></tr>
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</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CAPSD_CPVBM CAPSD_CPVBM]] Capsid protein self-assembles to form an icosahedral capsid with a pseudo T=2 symmetry, about 50 nm in diameter, and consisting of 120 capsid proteins. The capsid encapsulates the genomic RNA.
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[https://www.uniprot.org/uniprot/Q9E957_CPVBM Q9E957_CPVBM]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cnf ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cnf ConSurf].
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Cytoplasmic polyhedrosis virus (CPV) is unique within the Reoviridae family in having a turreted single-layer capsid contained within polyhedrin inclusion bodies, yet being fully capable of cell entry and endogenous RNA transcription. Biochemical data have shown that the amino-terminal 79 residues of the CPV turret protein (TP) is sufficient to bring CPV or engineered proteins into the polyhedrin matrix for micro-encapsulation. Here we report the three-dimensional structure of CPV at 3.88 A resolution using single-particle cryo-electron microscopy. Our map clearly shows the turns and deep grooves of alpha-helices, the strand separation in beta-sheets, and densities for loops and many bulky side chains; thus permitting atomic model-building effort from cryo-electron microscopy maps. We observed a helix-to-beta-hairpin conformational change between the two conformational states of the capsid shell protein in the region directly interacting with genomic RNA. We have also discovered a messenger RNA release hole coupled with the mRNA capping machinery unique to CPV. Furthermore, we have identified the polyhedrin-binding domain, a structure that has potential in nanobiotechnology applications.
 
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3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy.,Yu X, Jin L, Zhou ZH Nature. 2008 May 15;453(7193):415-9. Epub 2008 Apr 30. PMID:18449192<ref>PMID:18449192</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 3cnf" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bombyx mori cypovirus 1]]
[[Category: Bombyx mori cypovirus 1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jin, L]]
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[[Category: Jin L]]
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[[Category: Yu, X]]
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[[Category: Yu X]]
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[[Category: Zhou, Z H]]
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[[Category: Zhou ZH]]
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[[Category: Capsid protein]]
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[[Category: Cytoplasmic polyhedrosis virus]]
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[[Category: Guanylyltransferase domain]]
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[[Category: Icosahedral virus]]
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[[Category: Polyhedrin-binding domain]]
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[[Category: Turret protein]]
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[[Category: Virus]]
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Current revision

3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

3cnf, resolution 3.88Å

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