7nt8

From Proteopedia

(Difference between revisions)

Current revision

Influenza virus H3N2 nucleoprotein - R416A mutant

Structural highlights

7nt8 is a 2 chain structure with sequence from Influenza A virus (A/Northern Territory/60/1968(H3N2)) and Schistosoma japonicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.22Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GST26_SCHJA Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.NCAP_I68A6 Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.[HAMAP-Rule:MF_04070]

Publication Abstract from PubMed

Influenza A viruses of the H1N1 and H3N2 subtypes are responsible for seasonal epidemic events. The influenza nucleoprotein (NP) binds to the viral genomic RNA and is essential for its replication. Efforts are under way to produce therapeutics and vaccines targeting the NP. Despite this, no structure of an NP from an H3N2 virus has previously been determined. Here, the structure of the A/Northern Territory/60/1968 (H3N2) influenza virus NP is presented at 2.2 A resolution. The structure is highly similar to those of the A/WSN/1933 (H1N1) and A/Hong Kong/483/97 (H5N1) NPs. Nonconserved amino acids are widely dispersed both at the sequence and structural levels. A movement of the 73-90 RNA-binding loop is observed to be the key difference between the structure determined here and previous structures. The data presented here increase the understanding of structural conservation amongst influenza NPs and may aid in the design of universal interventions against influenza.

Structure of an H3N2 influenza virus nucleoprotein.,Knight ML, Fan H, Bauer DLV, Grimes JM, Fodor E, Keown JR Acta Crystallogr F Struct Biol Commun. 2021 Jul 1;77(Pt 7):208-214. doi:, 10.1107/S2053230X2100635X. Epub 2021 Jun 29. PMID:34196611^[1]

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

References

↑ Knight ML, Fan H, Bauer DLV, Grimes JM, Fodor E, Keown JR. Structure of an H3N2 influenza virus nucleoprotein. Acta Crystallogr F Struct Biol Commun. 2021 Jul 1;77(Pt 7):208-214. doi:, 10.1107/S2053230X2100635X. Epub 2021 Jun 29. PMID:34196611 doi:http://dx.doi.org/10.1107/S2053230X2100635X

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7nt8"

@@ Line 1: / Line 1: @@
 ==Influenza virus H3N2 nucleoprotein - R416A mutant==
-<StructureSection load='7nt8' size='340' side='right'caption='[[7nt8]]' scene=''>
+<StructureSection load='7nt8' size='340' side='right'caption='[[7nt8]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NT8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7nt8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Northern_Territory/60/1968(H3N2)) Influenza A virus (A/Northern Territory/60/1968(H3N2))] and [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NT8 FirstGlance]. <br>
-</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=7nt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nt8 OCA], [https://pdbe.org/7nt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nt8 RCSB], [https://www.ebi.ac.uk/pdbsum/7nt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nt8 ProSAT]</span></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]] 2.22&#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=7nt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nt8 OCA], [https://pdbe.org/7nt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nt8 RCSB], [https://www.ebi.ac.uk/pdbsum/7nt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nt8 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.  GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.[https://www.uniprot.org/uniprot/NCAP_I68A6 NCAP_I68A6] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.[HAMAP-Rule:MF_04070]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Influenza A viruses of the H1N1 and H3N2 subtypes are responsible for seasonal epidemic events. The influenza nucleoprotein (NP) binds to the viral genomic RNA and is essential for its replication. Efforts are under way to produce therapeutics and vaccines targeting the NP. Despite this, no structure of an NP from an H3N2 virus has previously been determined. Here, the structure of the A/Northern Territory/60/1968 (H3N2) influenza virus NP is presented at 2.2 A resolution. The structure is highly similar to those of the A/WSN/1933 (H1N1) and A/Hong Kong/483/97 (H5N1) NPs. Nonconserved amino acids are widely dispersed both at the sequence and structural levels. A movement of the 73-90 RNA-binding loop is observed to be the key difference between the structure determined here and previous structures. The data presented here increase the understanding of structural conservation amongst influenza NPs and may aid in the design of universal interventions against influenza.
+Structure of an H3N2 influenza virus nucleoprotein.,Knight ML, Fan H, Bauer DLV, Grimes JM, Fodor E, Keown JR Acta Crystallogr F Struct Biol Commun. 2021 Jul 1;77(Pt 7):208-214. doi:, 10.1107/S2053230X2100635X. Epub 2021 Jun 29. PMID:34196611<ref>PMID:34196611</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7nt8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
+*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
+[[Category: Schistosoma japonicum]]
 [[Category: Fodor E]]
 [[Category: Grimes JM]]
 [[Category: Keown JR]]
 [[Category: Knight ML]]

7nt8

From Proteopedia

Current revision

Influenza virus H3N2 nucleoprotein - R416A mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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