4cs7: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cs7]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CS7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cs7]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CS7 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cs8|4cs8]], [[4cs9|4cs9]], [[4csa|4csa]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cs8|4cs8]], [[4cs9|4cs9]], [[4csa|4csa]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cs7 RCSB], [http://www.ebi.ac.uk/pdbsum/4cs7 PDBsum]</span></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=4cs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cs7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cs7 RCSB], [http://www.ebi.ac.uk/pdbsum/4cs7 PDBsum]</span></td></tr>
<table>
</table>
<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: Grimes, J M.]]
[[Category: Grimes, J M]]
[[Category: Harlos, K.]]
[[Category: Harlos, K]]
[[Category: Leyrat, C.]]
[[Category: Leyrat, C]]
[[Category: Renner, M.]]
[[Category: Renner, M]]
[[Category: Antiterminator]]
[[Category: Antiterminator]]
[[Category: Asymmetric tetramer]]
[[Category: Asymmetric tetramer]]

Revision as of 16:13, 4 January 2015

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

4cs7 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. 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

4cs7, resolution 2.47Å

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