1jmu

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[[Image:1jmu.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the Reovirus mu1/sigma3 Complex==
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|PDB= 1jmu |SIZE=350|CAPTION= <scene name='initialview01'>1jmu</scene>, resolution 2.80&Aring;
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<StructureSection load='1jmu' size='340' side='right'caption='[[1jmu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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<table><tr><td colspan='2'>[[1jmu]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JMU FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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|GENE= M2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.]), S4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1jmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmu OCA], [https://pdbe.org/1jmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jmu RCSB], [https://www.ebi.ac.uk/pdbsum/1jmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmu ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of the Reovirus mu1/sigma3 Complex'''
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== Function ==
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[https://www.uniprot.org/uniprot/MU1_REOVL MU1_REOVL] Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref> The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jmu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1jmu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.
Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.
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==About this Structure==
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Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.,Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC Cell. 2002 Jan 25;108(2):283-95. PMID:11832217<ref>PMID:11832217</ref>
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1JMU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3., Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC, Cell. 2002 Jan 25;108(2):283-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11832217 11832217]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1jmu" style="background-color:#fffaf0;"></div>
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[[Category: Reovirus sp.]]
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[[Category: Harrison, S C.]]
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[[Category: Liemann, S.]]
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[[Category: Nibert, M L.]]
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[[Category: ACE]]
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[[Category: BOG]]
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[[Category: CL]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: jelly roll]]
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[[Category: protein-protein complex]]
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[[Category: zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:32 2008''
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Reovirus sp]]
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[[Category: Harrison SC]]
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[[Category: Liemann S]]
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[[Category: Nibert ML]]

Current revision

Crystal Structure of the Reovirus mu1/sigma3 Complex

PDB ID 1jmu

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