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2m0a

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Revision as of 10:57, 19 May 2021

Solution structure of MHV nsp3a

Structural highlights

2m0a is a 1 chain structure with sequence from Cvma5. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	1a (CVMA5)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[R1A_CVMA5] The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity). The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1-phosphate (ADRP)-binding function (By similarity). Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity). Nsp9 is a ssRNA-binding protein (By similarity).

Publication Abstract from PubMed

Coronaviruses (CoVs) are positive-sense, single-stranded, enveloped RNA viruses that infect a variety of vertebrate hosts. The CoV nucleocapsid (N) protein contains two structurally independent RNA binding domains denoted the N-terminal domain (NTD) and the dimeric C-terminal (CTD) domain joined by a charged linker region rich in serine and arginine residues (SR-rich linker). An important goal in unraveling N function is to molecularly characterize N-protein interactions. Recent genetic evidence suggests that N interacts with nsp3a, a component of the viral replicase. Here, we present the solution NMR structure of MHV nsp3a and show, using isothermal titration calorimetry, that MHV N219, an N construct that extends into the SR-rich linker (residues 60-219), binds cognate nsp3a with high affinity (K(a) = 1.4 (+/-0.3) x 10(6) M(-1)). In contrast, neither N197, an N construct containing only the folded NTD (residues 60-197), or the CTD dimer (residues 260-380), bind nsp3a with detectable affinity. This indicates that the key nsp3a binding determinants localize to the SR-rich linker, a finding consistent with reverse genetics studies. NMR chemical shift perturbation analysis reveals that the N-terminal region of an MHV N SR-rich linker peptide (residues 198-230) binds to the acidic face of MHV nsp3a containing the acidic alpha2 helix with an affinity K(a) of 8.3 x 10(3) M(-1). These studies reveal that the SR-rich linker of MHV N is necessary but not sufficient to maintain this high-affinity binding to N.

Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein.,Keane SC, Giedroc DP J Virol. 2013 Jan 9. PMID:23302895^[1]

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

References

↑ Keane SC, Giedroc DP. Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein. J Virol. 2013 Jan 9. PMID:23302895 doi:http://dx.doi.org/10.1128/JVI.03112-12

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/2m0a"

Categories: Cvma5 | Large Structures | Giedroc, D P | Keane, S C | Hydrolase

@@ Line 1: / Line 1: @@
 ==Solution structure of MHV nsp3a==
-<StructureSection load='2m0a' size='340' side='right' caption='[[2m0a]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
+<StructureSection load='2m0a' size='340' side='right'caption='[[2m0a]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2m0a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M0A FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2m0a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M0A FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m0a OCA], [http://pdbe.org/2m0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m0a RCSB], [http://www.ebi.ac.uk/pdbsum/2m0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m0a 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=2m0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m0a OCA], [https://pdbe.org/2m0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m0a RCSB], [https://www.ebi.ac.uk/pdbsum/2m0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m0a ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/R1A_CVMA5 R1A_CVMA5]] The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity).  The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).  Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).  Nsp9 is a ssRNA-binding protein (By similarity).
+[[https://www.uniprot.org/uniprot/R1A_CVMA5 R1A_CVMA5]] The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity).  The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).  Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter (By similarity).  Nsp9 is a ssRNA-binding protein (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[Category: Cvma5]]
+[[Category: Large Structures]]
 [[Category: Giedroc, D P]]
 [[Category: Keane, S C]]
 [[Category: Hydrolase]]

2m0a

From Proteopedia

Revision as of 10:57, 19 May 2021

Solution structure of MHV nsp3a

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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