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| | <StructureSection load='4cs8' size='340' side='right'caption='[[4cs8]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4cs8' size='340' side='right'caption='[[4cs8]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cs8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Hmpv Hmpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CS8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cs8]] 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=4CS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CS8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cs7|4cs7]], [[4cs9|4cs9]], [[4csa|4csa]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs8 OCA], [http://pdbe.org/4cs8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cs8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cs8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs8 ProSAT]</span></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=4cs8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs8 OCA], [https://pdbe.org/4cs8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cs8 RCSB], [https://www.ebi.ac.uk/pdbsum/4cs8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cs8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8QN58_9MONO Q8QN58_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: Hmpv]] | + | [[Category: Human metapneumovirus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grimes, J M]] | + | [[Category: Grimes JM]] |
| - | [[Category: Harlos, K]] | + | [[Category: Harlos K]] |
| - | [[Category: Leyrat, C]] | + | [[Category: Leyrat C]] |
| - | [[Category: Renner, M]] | + | [[Category: Renner M]] |
| - | [[Category: Antiterminator]]
| + | |
| - | [[Category: Asymmetric tetramer]]
| + | |
| - | [[Category: Modular protein]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Transcription elongation]]
| + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
Q8QN58_9MONO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM. Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae. Elife. 2014 May 19:e02674. doi: 10.7554/eLife.02674. PMID:24842877 doi:http://dx.doi.org/10.7554/eLife.02674
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