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5e06

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Revision as of 22:08, 28 June 2023

Structure of Sin Nombre virus nucleoprotein in long-axis crystal form

Structural highlights

5e06 is a 1 chain structure with sequence from Sin Nombre orthohantavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.001Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NCAP_SINV Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891).[UniProtKB:O36307][UniProtKB:P05133]^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

Publication Abstract from PubMed

Hantaviruses, which belong to the Hantavirus genus of the Bunyaviridae family, infect mammalian animals and humans, causing either hemorrhagic fever with renal syndrome (HFRS) or hantavirus cardiopulmonary syndrome (HCPS) in humans with high mortality. Hantavirus encodes a nucleocapsid protein (NP) to encapsidate genome and form a ribonucleoprotein complex (RNP) together with viral polymerase. Here, we report the crystal structure of the core domain of NP (NPcore) encoded by Sin Nombre virus (SNV) and Andes virus (ANDV), which are two representative members that cause HCPS in the New World. The constructs of SNV and ANDV NPcores exclude the N- and C-terminal portions of full polypeptide to get stable proteins for crystallographic study. The structure features an N-lobe and a C-lobe to clamp RNA-binding crevice, and presents two protruding extensions in both lobes. The positively charged residues located in RNA-binding crevice play a key role in RNA binding and virus replication. We further demonstrated that the C-terminal helix and the linker region connecting the N-terminal coiled-coil domain and NPcore are essential for hantavirus NP oligomerization through contacts made with two adjacent protomers. Moreover, EM visualization of native RNPs extracted from the virions revealed that a monomer-sized NP-RNA complex is the building block of viral RNP. This work provides insight into the formation of hantavirus RNP and provides an understanding of the evolutionary connections that exist amongst bunyaviruses. IMPORTANCE: Hantaviruses distribute in wide and increasing range of host reservoirs throughout the world. Particularly, hantaviruses can be transmitted via aerosols of rodent excreta to humans or human-to-human and cause HFRS and HCPS with mortalities of 15% and 50%, respectively. Hantaviruses are therefore listed as a category C pathogen. Hantavirus encodes an NP that plays essential roles both in RNP formation and in multiple biological functions. NP is also the exclusive target for the serological diagnoses. This work reveals the structure of hantavirus NP, furthering the knowledge of hantavirus RNP formation, revealing the relationship between hantavirus NP and serological specificity, and raising the potential for the development of new diagnosis and therapeutics targeting hantavirus infection.

Crystal structure of the core region of hantavirus nucleocapsid protein reveals the mechanism for ribonucleoprotein complex formation.,Guo Y, Wang W, Sun Y, Ma C, Wang X, Wang X, Liu P, Shen S, Li B, Lin J, Deng F, Wang H, Lou Z J Virol. 2015 Nov 11. pii: JVI.02523-15. PMID:26559827^[12]

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

References

↑ Mir MA, Panganiban AT. Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle. J Virol. 2004 Aug;78(15):8281-8. PMID:15254200 doi:10.1128/JVI.78.15.8281-8288.2004
↑ Mir MA, Panganiban AT. The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding. J Virol. 2005 Feb;79(3):1824-35. PMID:15650206 doi:10.1128/JVI.79.3.1824-1835.2005
↑ Mir MA, Panganiban AT. Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein. J Virol. 2006 Jul;80(13):6276-85. PMID:16775315 doi:10.1128/JVI.00147-06
↑ Mir MA, Brown B, Hjelle B, Duran WA, Panganiban AT. Hantavirus N protein exhibits genus-specific recognition of the viral RNA panhandle. J Virol. 2006 Nov;80(22):11283-92. PMID:16971445 doi:10.1128/JVI.00820-06
↑ Mir MA, Panganiban AT. A protein that replaces the entire cellular eIF4F complex. EMBO J. 2008 Dec 3;27(23):3129-39. PMID:18971945 doi:10.1038/emboj.2008.228
↑ Mir MA, Duran WA, Hjelle BL, Ye C, Panganiban AT. Storage of cellular 5' mRNA caps in P bodies for viral cap-snatching. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19294-9. PMID:19047634 doi:10.1073/pnas.0807211105
↑ Mir MA, Sheema S, Haseeb A, Haque A. Hantavirus nucleocapsid protein has distinct m7G cap J Biol Chem. 2010 Apr 9;285(15):11357-68. PMID:20164193 doi:10.1074/jbc.M110.102459
↑ Haque A, Mir MA. Interaction of hantavirus nucleocapsid protein with ribosomal protein S19. J Virol. 2010 Dec;84(23):12450-3. PMID:20844026 doi:10.1128/JVI.01388-10
↑ Brown BA, Panganiban AT. Identification of a region of hantavirus nucleocapsid protein required for RNA chaperone activity. RNA Biol. 2010 Nov-Dec;7(6):830-7. PMID:21378500 doi:10.4161/rna.7.6.13862
↑ Ganaie SS, Haque A, Cheng E, Bonny TS, Salim NN, Mir MA. Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism. Biochem J. 2014 Nov 15;464(1):109-21. PMID:25062117 doi:10.1042/BJ20140449
↑ Möncke-Buchner E, Szczepek M, Bokelmann M, Heinemann P, Raftery MJ, Krüger DH, Reuter M. Sin Nombre hantavirus nucleocapsid protein exhibits a metal-dependent DNA-specific endonucleolytic activity. Virology. 2016 Sep;496:67-76. PMID:27261891 doi:10.1016/j.virol.2016.05.009
↑ Guo Y, Wang W, Sun Y, Ma C, Wang X, Wang X, Liu P, Shen S, Li B, Lin J, Deng F, Wang H, Lou Z. Crystal structure of the core region of hantavirus nucleocapsid protein reveals the mechanism for ribonucleoprotein complex formation. J Virol. 2015 Nov 11. pii: JVI.02523-15. PMID:26559827 doi:http://dx.doi.org/10.1128/JVI.02523-15

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/5e06"

Categories: Large Structures | Sin Nombre orthohantavirus | Guo Y | Lou ZY | Wang WM

@@ Line 3: / Line 3: @@
 <StructureSection load='5e06' size='340' side='right'caption='[[5e06]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5e06]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E06 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E06 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5e06]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sin_Nombre_orthohantavirus Sin Nombre orthohantavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E06 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e04|5e04]], [[5e05|5e05]], [[5e07|5e07]]</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]] 3.001&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e06 OCA], [http://pdbe.org/5e06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e06 RCSB], [http://www.ebi.ac.uk/pdbsum/5e06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e06 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=5e06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e06 OCA], [https://pdbe.org/5e06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e06 RCSB], [https://www.ebi.ac.uk/pdbsum/5e06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e06 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/NCAP_SINV NCAP_SINV] Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891).[UniProtKB:O36307][UniProtKB:P05133]<ref>PMID:15254200</ref> <ref>PMID:15650206</ref> <ref>PMID:16775315</ref> <ref>PMID:16971445</ref> <ref>PMID:18971945</ref> <ref>PMID:19047634</ref> <ref>PMID:20164193</ref> <ref>PMID:20844026</ref> <ref>PMID:21378500</ref> <ref>PMID:25062117</ref> <ref>PMID:27261891</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Guo, Y]]
+[[Category: Sin Nombre orthohantavirus]]
-[[Category: Lou, Z Y]]
+[[Category: Guo Y]]
-[[Category: Wang, W M]]
+[[Category: Lou ZY]]
-[[Category: Hantavirus]]
+[[Category: Wang WM]]
-[[Category: Nuclear protein]]
-[[Category: Nucleoprotein]]
-[[Category: Sin nombre virus]]

5e06

From Proteopedia

Revision as of 22:08, 28 June 2023

Structure of Sin Nombre virus nucleoprotein in long-axis crystal form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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