1mbm

From Proteopedia

(Difference between revisions)

Revision as of 10:06, 25 October 2017

NSP4 proteinase from Equine Arteritis Virus

Structural highlights

1mbm is a 4 chain structure with sequence from Eav. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1cqq, 1hav, 1l1n, 1hpg
Gene:	NSP4 (EAV)
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.

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^[6]

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

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:http://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:http://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:http://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:http://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:http://dx.doi.org/10.1016/j.chom.2007.09.014
↑ Barrette-Ng IH, Ng KK, Mark BL, Van Aken D, Cherney MM, Garen C, Kolodenko Y, Gorbalenya AE, Snijder EJ, James MN. Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole. J Biol Chem. 2002 Oct 18;277(42):39960-6. Epub 2002 Aug 5. PMID:12163505 doi:10.1074/jbc.M206978200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mbm"

@@ 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=''>
@@ Line 5: / Line 6: @@
 </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>
 <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'>[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]</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 ==
@@ Line 17: / Line 18: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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;">

1mbm

From Proteopedia

Revision as of 10:06, 25 October 2017

NSP4 proteinase from Equine Arteritis Virus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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