4cs7: Difference between revisions
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==Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1== | |||
<StructureSection load='4cs7' size='340' side='right'caption='[[4cs7]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4cs7]] 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=4CS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CS7 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]] 2.47Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4cs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs7 OCA], [https://pdbe.org/4cs7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cs7 RCSB], [https://www.ebi.ac.uk/pdbsum/4cs7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8QN58_9MONO Q8QN58_9MONO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The M2-1 protein of human metapneumovirus (HMPV) is a zinc-binding transcription antiterminator which is highly conserved among pneumoviruses. We report the structure of tetrameric HMPV M2-1. Each protomer features a N-terminal zinc finger domain and an alpha-helical tetramerization motif forming a rigid unit, followed by a flexible linker and an alpha-helical core domain. The tetramer is asymmetric, three of the protomers exhibiting a closed conformation, and one an open conformation. Molecular dynamics simulations and SAXS demonstrate a dynamic equilibrium between open and closed conformations in solution. Structures of adenosine monophosphate- and DNA- bound M2-1 establish the role of the zinc finger domain in base-specific recognition of RNA. Binding to 'gene end' RNA sequences stabilized the closed conformation of M2-1 leading to a drastic shift in the conformational landscape of M2-1. We propose a model for recognition of gene end signals and discuss the implications of these findings for transcriptional regulation in pneumoviruses. | |||
Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae.,Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM Elife. 2014 May 19:e02674. doi: 10.7554/eLife.02674. PMID:24842877<ref>PMID:24842877</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cs7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human metapneumovirus]] | |||
[[Category: Large Structures]] | |||
[[Category: Grimes JM]] | |||
[[Category: Harlos K]] | |||
[[Category: Leyrat C]] | |||
[[Category: Renner M]] | |||
Latest revision as of 14:14, 9 May 2024
Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1
Structural highlights
FunctionPublication Abstract from PubMedThe M2-1 protein of human metapneumovirus (HMPV) is a zinc-binding transcription antiterminator which is highly conserved among pneumoviruses. We report the structure of tetrameric HMPV M2-1. Each protomer features a N-terminal zinc finger domain and an alpha-helical tetramerization motif forming a rigid unit, followed by a flexible linker and an alpha-helical core domain. The tetramer is asymmetric, three of the protomers exhibiting a closed conformation, and one an open conformation. Molecular dynamics simulations and SAXS demonstrate a dynamic equilibrium between open and closed conformations in solution. Structures of adenosine monophosphate- and DNA- bound M2-1 establish the role of the zinc finger domain in base-specific recognition of RNA. Binding to 'gene end' RNA sequences stabilized the closed conformation of M2-1 leading to a drastic shift in the conformational landscape of M2-1. We propose a model for recognition of gene end signals and discuss the implications of these findings for transcriptional regulation in pneumoviruses. Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae.,Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM Elife. 2014 May 19:e02674. doi: 10.7554/eLife.02674. PMID:24842877[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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