5y3d: Difference between revisions
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==Structural insight into the interaction between RNA polymerase and VPg for norovirus replication== | |||
<StructureSection load='5y3d' size='340' side='right'caption='[[5y3d]], [[Resolution|resolution]] 3.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5y3d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_norovirus Murine norovirus] and [https://en.wikipedia.org/wiki/Murine_norovirus_1 Murine norovirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y3D 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]] 3.14Å</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=5y3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y3d OCA], [https://pdbe.org/5y3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y3d RCSB], [https://www.ebi.ac.uk/pdbsum/5y3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y3d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q80J95_9CALI Q80J95_9CALI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Norovirus (NoV) is a leading cause of epidemic acute non-bacterial gastroenteritis, and replicates through virion protein genome-linked (VPg)-primed or de novo RNA synthesis by RNA-dependent RNA polymerase (RdRp). VPg is a multifunctional protein that plays crucial roles in viral protein translation and genome replication. However, the interaction between the RdRp and this multifunctional VPg in NoV replication has been unknown. In this study, VPg derived from murine NoV (MNV) was found to mediate the formation of higher-order multimers or tubular fibrils of MNV RdRp, which led to significantly enhanced polymerase activity in vitro. The replication of MNV mutants containing a VPg-binding defective RdRp, based on the crystal structure of an RdRp-VPg(1-73) complex, was completely blocked in a cell culture system. Our data suggest that the interaction between RdRp and VPg plays a crucial role in the multimerization-mediated RdRp activity in vivo and consequently in MNV replication, which can provide a new target of therapeutic intervention for NoV outbreaks. | |||
Insight Into the Interaction Between RNA Polymerase and VPg for Murine Norovirus Replication.,Lee JH, Park BS, Han KR, Biering SB, Kim SJ, Choi J, Seok JH, Alam I, Chung MS, Kim HM, Hwang S, Kim KH Front Microbiol. 2018 Jul 3;9:1466. doi: 10.3389/fmicb.2018.01466. eCollection, 2018. PMID:30038601<ref>PMID:30038601</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5y3d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Murine norovirus]] | |||
[[Category: Murine norovirus 1]] | |||
[[Category: Kim KH]] | |||
[[Category: Lee J-H]] | |||
[[Category: Seok JH]] | |||
Latest revision as of 11:20, 22 November 2023
Structural insight into the interaction between RNA polymerase and VPg for norovirus replicationStructural insight into the interaction between RNA polymerase and VPg for norovirus replication
Structural highlights
FunctionPublication Abstract from PubMedNorovirus (NoV) is a leading cause of epidemic acute non-bacterial gastroenteritis, and replicates through virion protein genome-linked (VPg)-primed or de novo RNA synthesis by RNA-dependent RNA polymerase (RdRp). VPg is a multifunctional protein that plays crucial roles in viral protein translation and genome replication. However, the interaction between the RdRp and this multifunctional VPg in NoV replication has been unknown. In this study, VPg derived from murine NoV (MNV) was found to mediate the formation of higher-order multimers or tubular fibrils of MNV RdRp, which led to significantly enhanced polymerase activity in vitro. The replication of MNV mutants containing a VPg-binding defective RdRp, based on the crystal structure of an RdRp-VPg(1-73) complex, was completely blocked in a cell culture system. Our data suggest that the interaction between RdRp and VPg plays a crucial role in the multimerization-mediated RdRp activity in vivo and consequently in MNV replication, which can provide a new target of therapeutic intervention for NoV outbreaks. Insight Into the Interaction Between RNA Polymerase and VPg for Murine Norovirus Replication.,Lee JH, Park BS, Han KR, Biering SB, Kim SJ, Choi J, Seok JH, Alam I, Chung MS, Kim HM, Hwang S, Kim KH Front Microbiol. 2018 Jul 3;9:1466. doi: 10.3389/fmicb.2018.01466. eCollection, 2018. PMID:30038601[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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