5m1m: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 5m1m is ON HOLD until Paper Publication Authors: Radzimanowski, J., Weissenhorn, W. Description: Crystal structure of matrix protein 1 from Influen... |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)== | |||
<StructureSection load='5m1m' size='340' side='right'caption='[[5m1m]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5m1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_C_virus_(C/Ann_Arbor/1/50) Influenza C virus (C/Ann Arbor/1/50)]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5M1M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5m1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1m OCA], [https://pdbe.org/5m1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m1m RCSB], [https://www.ebi.ac.uk/pdbsum/5m1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5m1m" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Radzimanowski J]] | |||
[[Category: Weissenhorn W]] | |||
Latest revision as of 18:20, 1 November 2023
Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)
| ||||||||||||
