7lj3

From Proteopedia

(Difference between revisions)

Current revision

Structure of human transfer RNA visualized in the cytomegalovirus, a DNA virus

Structural highlights

7lj3 is a 12 chain structure with sequence from Homo sapiens and Human herpesvirus 5 strain AD169. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.9Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PP150_HCMVA Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Under the Baltimore nucleic acid-based virus classification scheme, the herpesvirus human cytomegalovirus (HCMV) is a Class I virus, meaning that it contains a double-stranded DNA genome-and no RNA. Here, we report sub-particle cryoEM reconstructions of HCMV virions at 2.9 A resolution revealing structures resembling non-coding transfer RNAs (tRNAs) associated with the virion's capsid-bound tegument protein, pp150. Through deep sequencing, we show that these RNA sequences match human tRNAs, and we built atomic models using the most abundant tRNA species. Based on our models, tRNA recruitment is mediated by the electrostatic interactions between tRNA phosphate groups and the helix-loop-helix motif of HCMV pp150. The specificity of these interactions may explain the absence of such tRNA densities in murine cytomegalovirus and other human herpesviruses.

Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150.,Liu YT, Strugatsky D, Liu W, Zhou ZH Nat Commun. 2021 Sep 17;12(1):5513. doi: 10.1038/s41467-021-25791-1. PMID:34535641^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ AuCoin DP, Smith GB, Meiering CD, Mocarski ES. Betaherpesvirus-conserved cytomegalovirus tegument protein ppUL32 (pp150) controls cytoplasmic events during virion maturation. J Virol. 2006 Aug;80(16):8199-210. PMID:16873276 doi:http://dx.doi.org/10.1128/JVI.00457-06
↑ Tandon R, Mocarski ES. Control of cytoplasmic maturation events by cytomegalovirus tegument protein pp150. J Virol. 2008 Oct;82(19):9433-44. doi: 10.1128/JVI.00533-08. Epub 2008 Jul 23. PMID:18653449 doi:http://dx.doi.org/10.1128/JVI.00533-08
↑ Indran SV, Britt WJ. A role for the small GTPase Rab6 in assembly of human cytomegalovirus. J Virol. 2011 May;85(10):5213-9. doi: 10.1128/JVI.02605-10. Epub 2011 Mar 16. PMID:21411515 doi:http://dx.doi.org/10.1128/JVI.02605-10
↑ Dai X, Yu X, Gong H, Jiang X, Abenes G, Liu H, Shivakoti S, Britt WJ, Zhu H, Liu F, Zhou ZH. The smallest capsid protein mediates binding of the essential tegument protein pp150 to stabilize DNA-containing capsids in human cytomegalovirus. PLoS Pathog. 2013 Aug;9(8):e1003525. doi: 10.1371/journal.ppat.1003525. Epub 2013, Aug 15. PMID:23966856 doi:http://dx.doi.org/10.1371/journal.ppat.1003525
↑ Bogdanow B, Weisbach H, von Einem J, Straschewski S, Voigt S, Winkler M, Hagemeier C, Wiebusch L. Human cytomegalovirus tegument protein pp150 acts as a cyclin A2-CDK-dependent sensor of the host cell cycle and differentiation state. Proc Natl Acad Sci U S A. 2013 Oct 22;110(43):17510-5. doi:, 10.1073/pnas.1312235110. Epub 2013 Oct 7. PMID:24101496 doi:http://dx.doi.org/10.1073/pnas.1312235110
↑ Liu YT, Strugatsky D, Liu W, Zhou ZH. Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150. Nat Commun. 2021 Sep 17;12(1):5513. PMID:34535641 doi:10.1038/s41467-021-25791-1

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7lj3"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7lj3 is ON HOLD  until Paper Publication
+==Structure of human transfer RNA visualized in the cytomegalovirus, a DNA virus==
+<StructureSection load='7lj3' size='340' side='right'caption='[[7lj3]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7lj3]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJ3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</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=7lj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lj3 OCA], [https://pdbe.org/7lj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lj3 RCSB], [https://www.ebi.ac.uk/pdbsum/7lj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lj3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PP150_HCMVA PP150_HCMVA] Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells.<ref>PMID:16873276</ref> <ref>PMID:18653449</ref> <ref>PMID:21411515</ref> <ref>PMID:23966856</ref> <ref>PMID:24101496</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Under the Baltimore nucleic acid-based virus classification scheme, the herpesvirus human cytomegalovirus (HCMV) is a Class I virus, meaning that it contains a double-stranded DNA genome-and no RNA. Here, we report sub-particle cryoEM reconstructions of HCMV virions at 2.9 A resolution revealing structures resembling non-coding transfer RNAs (tRNAs) associated with the virion's capsid-bound tegument protein, pp150. Through deep sequencing, we show that these RNA sequences match human tRNAs, and we built atomic models using the most abundant tRNA species. Based on our models, tRNA recruitment is mediated by the electrostatic interactions between tRNA phosphate groups and the helix-loop-helix motif of HCMV pp150. The specificity of these interactions may explain the absence of such tRNA densities in murine cytomegalovirus and other human herpesviruses.
-Authors:
+Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150.,Liu YT, Strugatsky D, Liu W, Zhou ZH Nat Commun. 2021 Sep 17;12(1):5513. doi: 10.1038/s41467-021-25791-1. PMID:34535641<ref>PMID:34535641</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7lj3" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Human herpesvirus 5 strain AD169]]
+[[Category: Large Structures]]
+[[Category: Liu W]]
+[[Category: Liu YT]]
+[[Category: Strugatsky D]]
+[[Category: Zhou ZH]]

7lj3

From Proteopedia

Current revision

Structure of human transfer RNA visualized in the cytomegalovirus, a DNA virus

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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