4lp7: Difference between revisions
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==Crystal structure of the human metapneumovirus matrix protein== | ==Crystal structure of the human metapneumovirus matrix protein== | ||
<StructureSection load='4lp7' size='340' side='right' caption='[[4lp7]], [[Resolution|resolution]] 2.83Å' scene=''> | <StructureSection load='4lp7' size='340' side='right'caption='[[4lp7]], [[Resolution|resolution]] 2.83Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lp7]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lp7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_metapneumovirus Human metapneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LP7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lp7 OCA], [https://pdbe.org/4lp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lp7 RCSB], [https://www.ebi.ac.uk/pdbsum/4lp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lp7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q91F56_9MONO Q91F56_9MONO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human metapneumovirus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Grimes JM]] | ||
[[Category: | [[Category: Harlos K]] | ||
[[Category: | [[Category: Leyrat C]] | ||
Latest revision as of 19:22, 20 September 2023
Crystal structure of the human metapneumovirus matrix proteinCrystal structure of the human metapneumovirus matrix protein
Structural highlights
FunctionPublication Abstract from PubMedThe matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 A resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca2+ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca2+ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses. Structure and Self-Assembly of the Calcium Binding Matrix Protein of Human Metapneumovirus.,Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM Structure. 2013 Dec 3. pii: S0969-2126(13)00425-5. doi:, 10.1016/j.str.2013.10.013. PMID:24316400[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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