2mch: Difference between revisions
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== | ==Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 CW3 WT== | ||
[[2mch]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCH OCA]. | <StructureSection load='2mch' size='340' side='right'caption='[[2mch]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MCH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mch OCA], [https://pdbe.org/2mch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mch RCSB], [https://www.ebi.ac.uk/pdbsum/2mch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mch ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q80J95_9CALI Q80J95_9CALI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Compact viral genomes such as those found in noroviruses, which cause significant enteric disease in humans, often encode only a few proteins, but affect a wide range of processes in their hosts and ensure efficient propagation of the virus. Both human and mouse noroviruses persistently replicate and are shed in stool, a highly effective strategy for spreading between hosts. For mouse norovirus (MNV), the presence of a glutamate rather than an aspartate at position 94 of the NS1/2 protein was previously shown to be essential for persistent replication and shedding. Here, we analyze these critical sequences of NS1/2 at the structural level. Using solution NMR methods we determined folded NS1/2 domain structures from a nonpersistent murine norovirus strain CW3, a persistent strain CR6, and a persistent mutant strain CW3D94E . We found an unstructured PEST-like domain followed by a novel folded domain in the N-terminus of NS1/2. All three forms of the domain are stable and monomeric in solution. Residue 94, critical for determining persistence, is located in a reverse turn following an alpha-helix in the folded domain. The longer sidechain of glutamate, but not aspartate, allows interaction with the indole group of the nearby tryptophan, reshaping the surface of the domain. The discrimination between glutamyl and aspartyl residue is imposed by the stable tertiary conformation. These structural requirements correlate with the in vivo function of NS1/2 in persistence, a key element of norovirus biology and infection. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. | |||
Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain.,Borin BN, Tang W, Nice TJ, McCune BT, Virgin HW, Krezel AM Proteins. 2013 Nov 25. doi: 10.1002/prot.24484. PMID:24273131<ref>PMID:24273131</ref> | |||
<ref | |||
[[ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 2mch" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Murine norovirus 1]] | |||
[[Category: Borin B]] | |||
[[Category: Krezel AM]] | |||
Latest revision as of 09:03, 15 May 2024
Backbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 CW3 WTBackbone 1H, 13C, and 15N Chemical Shift Assignments for murine norovirus NS1/2 CW3 WT
Structural highlights
FunctionPublication Abstract from PubMedCompact viral genomes such as those found in noroviruses, which cause significant enteric disease in humans, often encode only a few proteins, but affect a wide range of processes in their hosts and ensure efficient propagation of the virus. Both human and mouse noroviruses persistently replicate and are shed in stool, a highly effective strategy for spreading between hosts. For mouse norovirus (MNV), the presence of a glutamate rather than an aspartate at position 94 of the NS1/2 protein was previously shown to be essential for persistent replication and shedding. Here, we analyze these critical sequences of NS1/2 at the structural level. Using solution NMR methods we determined folded NS1/2 domain structures from a nonpersistent murine norovirus strain CW3, a persistent strain CR6, and a persistent mutant strain CW3D94E . We found an unstructured PEST-like domain followed by a novel folded domain in the N-terminus of NS1/2. All three forms of the domain are stable and monomeric in solution. Residue 94, critical for determining persistence, is located in a reverse turn following an alpha-helix in the folded domain. The longer sidechain of glutamate, but not aspartate, allows interaction with the indole group of the nearby tryptophan, reshaping the surface of the domain. The discrimination between glutamyl and aspartyl residue is imposed by the stable tertiary conformation. These structural requirements correlate with the in vivo function of NS1/2 in persistence, a key element of norovirus biology and infection. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain.,Borin BN, Tang W, Nice TJ, McCune BT, Virgin HW, Krezel AM Proteins. 2013 Nov 25. doi: 10.1002/prot.24484. PMID:24273131[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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