5m1m

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m (Protected "5m1m" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5m1m is ON HOLD until Paper Publication
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==Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)==
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<StructureSection load='5m1m' size='340' side='right' caption='[[5m1m]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5m1m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M1M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<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=5m1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1m OCA], [http://pdbe.org/5m1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m1m RCSB], [http://www.ebi.ac.uk/pdbsum/5m1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/MAT_INCAA MAT_INCAA]] Ion channel, which might have a role in genome packaging and uncoating processes.<ref>PMID:21106743</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Matrix proteins from enveloped viruses play an important role in budding and stabilizing virus particles. In order to assess the role of the matrix protein M1 from influenza C virus (M1-C) in plasma membrane deformation, we have combined structural and in vitro reconstitution experiments with model membranes. We present the crystal structure of the N-terminal domain of M1-C and show by Small Angle X-Ray Scattering analysis that full-length M1-C folds into an elongated structure that associates laterally into ring-like or filamentous polymers. Using negatively charged giant unilamellar vesicles (GUVs), we demonstrate that M1-C full-length binds to and induces inward budding of membrane tubules with diameters that resemble the diameter of viruses. Membrane tubule formation requires the C-terminal domain of M1-C, corroborating its essential role for M1-C polymerization. Our results indicate that M1-C assembly on membranes constitutes the driving force for budding and suggest that M1-C plays a key role in facilitating viral egress.
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Authors: Radzimanowski, J., Weissenhorn, W.
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The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.,Saletti D, Radzimanowski J, Effantin G, Midtvedt D, Mangenot S, Weissenhorn W, Bassereau P, Bally M Sci Rep. 2017 Jan 25;7:40801. doi: 10.1038/srep40801. PMID:28120862<ref>PMID:28120862</ref>
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Description: Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Weissenhorn, W]]
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<div class="pdbe-citations 5m1m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Radzimanowski, J]]
[[Category: Radzimanowski, J]]
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[[Category: Weissenhorn, W]]
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[[Category: Influenza c]]
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[[Category: Matrix protein 1]]
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[[Category: Viral protein]]

Revision as of 09:27, 10 March 2017

Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)

5m1m, resolution 1.50Å

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