1mbm: Difference between revisions

Latest revision as of 07:42, 14 February 2024

NSP4 proteinase from Equine Arteritis Virus

Structural highlights

1mbm is a 4 chain structure with sequence from Equine arteritis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOA_EAVBU The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.^[1] Nsp1 is essential for viral subgenomic mRNA synthesis.^[2] Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.^[3] The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.^[4] The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014
↑ Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014
↑ Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014
↑ Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014
↑ Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

[2] Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

[3] Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

[4] Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

[5] Frias-Staheli N, Giannakopoulos NV, Kikkert M, Taylor SL, Bridgen A, Paragas J, Richt JA, Rowland RR, Schmaljohn CS, Lenschow DJ, Snijder EJ, Garcia-Sastre A, Virgin HW 4th. Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses. Cell Host Microbe. 2007 Dec 13;2(6):404-16. PMID:18078692 doi:https://dx.doi.org/10.1016/j.chom.2007.09.014

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@@ Line 1: / Line 1: @@
 ==NSP4 proteinase from Equine Arteritis Virus==
-<StructureSection load='1mbm' size='340' side='right' caption='[[1mbm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1mbm' size='340' side='right'caption='[[1mbm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mbm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eav Eav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mbm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_arteritis_virus Equine arteritis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cqq|1cqq]], [[1hav|1hav]], [[1l1n|1l1n]], [[1hpg|1hpg]]</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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NSP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11047 EAV])</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=1mbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbm OCA], [https://pdbe.org/1mbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbm RCSB], [https://www.ebi.ac.uk/pdbsum/1mbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbm ProSAT]</span></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=1mbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbm OCA], [http://pdbe.org/1mbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mbm RCSB], [http://www.ebi.ac.uk/pdbsum/1mbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU]] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref>   Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref>   Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref>   The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref>   The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>
+[https://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref>   Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref>   Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref>   The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref>   The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mbm ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Arteriviruses are enveloped, positive-stranded RNA viruses and include pathogens of major economic concern to the swine- and horse-breeding industries. The arterivirus replicase gene encodes two large precursor polyproteins that are processed by the viral main proteinase nonstructural protein 4 (nsp4). The three-dimensional structure of the 21-kDa nsp4 from the arterivirus prototype equine arteritis virus has been determined to 2.0 A resolution. Nsp4 adopts the smallest known chymotrypsin-like fold with a canonical catalytic triad of Ser-120, His-39, and Asp-65, as well as a novel alpha/beta C-terminal extension domain that may play a role in mediating protein-protein interactions. In different copies of nsp4 in the asymmetric unit, the oxyanion hole adopts either a collapsed inactive conformation or the standard active conformation, which may be a novel way of regulating proteolytic activity.
-Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole.,Barrette-Ng IH, Ng KK, Mark BL, Van Aken D, Cherney MM, Garen C, Kolodenko Y, Gorbalenya AE, Snijder EJ, James MN J Biol Chem. 2002 Oct 18;277(42):39960-6. Epub 2002 Aug 5. PMID:12163505<ref>PMID:12163505</ref>
+==See Also==
+*[[Proteinase 3D structures|Proteinase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mbm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Eav]]
+[[Category: Equine arteritis virus]]
-[[Category: Aken, D van]]
+[[Category: Large Structures]]
-[[Category: Barrette-Ng, I H]]
+[[Category: Barrette-Ng IH]]
-[[Category: Cherney, M M]]
+[[Category: Cherney MM]]
-[[Category: Garen, C]]
+[[Category: Garen C]]
-[[Category: Gorbalenya, A E]]
+[[Category: Gorbalenya AE]]
-[[Category: James, M N.G]]
+[[Category: James MNG]]
-[[Category: Kolodenko, Y]]
+[[Category: Kolodenko Y]]
-[[Category: Mark, B L]]
+[[Category: Mark BL]]
-[[Category: Ng, K K.S]]
+[[Category: Ng KK-S]]
-[[Category: Snijder, E J]]
+[[Category: Snijder EJ]]
-[[Category: Chymotrypsin-like proteinase]]
+[[Category: Van Aken D]]
-[[Category: Collapsed oxyanion hole]]
-[[Category: Serine proteinase]]
-[[Category: Transferase]]

1mbm: Difference between revisions

Latest revision as of 07:42, 14 February 2024

NSP4 proteinase from Equine Arteritis Virus

Structural highlights

Function

Evolutionary Conservation

See Also

References

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