4dwc

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the glycoprotein Erns from the pestivirus BVDV-1 in complex with Zn ions

Structural highlights

4dwc is a 2 chain structure with sequence from Bovine viral diarrhea virus 1-CP7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.89Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

POLG_BVDVC Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity). P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity). Uncleaved NS2-3 is required for production of infectious virus. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity (By similarity). RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.

Publication Abstract from PubMed

Pestiviruses, which belong to the Flaviviridae family of RNA viruses, are important agents of veterinary diseases causing substantial economical losses in animal farming worldwide. Pestivirus particles display three envelope glycoproteins at their surface: E(rns), E1, and E2. We report here the crystal structure of the catalytic domain of E(rns), the ribonucleolytic activity of which is believed to counteract the innate immunity of the host. The structure reveals a three-dimensional fold corresponding to T2 ribonucleases from plants and fungi. Cocrystallization experiments with mono- and oligonucleotides revealed the structural basis for substrate recognition at two binding sites previously identified for T2 RNases. A detailed analysis of poly-U cleavage products using (31)P-NMR and size exclusion chromatography, together with molecular docking studies, provides a comprehensive mechanistic picture of E(rns) activity on its substrates and reveals the presence of at least one additional nucleotide binding site.

Crystal Structure of the Pestivirus Envelope Glycoprotein E(rns) and Mechanistic Analysis of Its Ribonuclease Activity.,Krey T, Bontems F, Vonrhein C, Vaney MC, Bricogne G, Rumenapf T, Rey FA Structure. 2012 May 9;20(5):862-73. PMID:22579253^[1]

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

References

↑ Krey T, Bontems F, Vonrhein C, Vaney MC, Bricogne G, Rumenapf T, Rey FA. Crystal Structure of the Pestivirus Envelope Glycoprotein E(rns) and Mechanistic Analysis of Its Ribonuclease Activity. Structure. 2012 May 9;20(5):862-73. PMID:22579253 doi:10.1016/j.str.2012.03.018

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/4dwc"

@@ Line 1: / Line 1: @@
-[[Image:4dwc.jpg|left|200px]]
-<!--
+==Crystal structure of the glycoprotein Erns from the pestivirus BVDV-1 in complex with Zn ions==
-The line below this paragraph, containing "STRUCTURE_4dwc", creates the "Structure Box" on the page.
+<StructureSection load='4dwc' size='340' side='right'caption='[[4dwc]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[4dwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_viral_diarrhea_virus_1-CP7 Bovine viral diarrhea virus 1-CP7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DWC FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_4dwc|  PDB=4dwc  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwc OCA], [https://pdbe.org/4dwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dwc RCSB], [https://www.ebi.ac.uk/pdbsum/4dwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/POLG_BVDVC POLG_BVDVC] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (By similarity).  P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity).  Uncleaved NS2-3 is required for production of infectious virus.  NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.  NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.  NS4A is a cofactor for the NS3 protease activity (By similarity).  RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pestiviruses, which belong to the Flaviviridae family of RNA viruses, are important agents of veterinary diseases causing substantial economical losses in animal farming worldwide. Pestivirus particles display three envelope glycoproteins at their surface: E(rns), E1, and E2. We report here the crystal structure of the catalytic domain of E(rns), the ribonucleolytic activity of which is believed to counteract the innate immunity of the host. The structure reveals a three-dimensional fold corresponding to T2 ribonucleases from plants and fungi. Cocrystallization experiments with mono- and oligonucleotides revealed the structural basis for substrate recognition at two binding sites previously identified for T2 RNases. A detailed analysis of poly-U cleavage products using (31)P-NMR and size exclusion chromatography, together with molecular docking studies, provides a comprehensive mechanistic picture of E(rns) activity on its substrates and reveals the presence of at least one additional nucleotide binding site.
-===Crystal structure of the glycoprotein Erns from the pestivirus BVDV-1 in complex with Zn ions===
+Crystal Structure of the Pestivirus Envelope Glycoprotein E(rns) and Mechanistic Analysis of Its Ribonuclease Activity.,Krey T, Bontems F, Vonrhein C, Vaney MC, Bricogne G, Rumenapf T, Rey FA Structure. 2012 May 9;20(5):862-73. PMID:22579253<ref>PMID:22579253</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_22579253}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 4dwc" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 22579253 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_22579253}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Bovine viral diarrhea virus 1-CP7]]
-[[4dwc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovine_viral_diarrhea_virus_1 Bovine viral diarrhea virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWC OCA].
+[[Category: Large Structures]]
+[[Category: Bontems F]]
-==Reference==
+[[Category: Bricogne G]]
-<ref group="xtra">PMID:022579253</ref><references group="xtra"/>
+[[Category: Krey T]]
-[[Category: Bovine viral diarrhea virus 1]]
+[[Category: Rey FA]]
-[[Category: Bontems, F.]]
+[[Category: Ruemenapf T]]
-[[Category: Bricogne, G.]]
+[[Category: Vaney M-C]]
-[[Category: Krey, T.]]
+[[Category: Vonrhein C]]
-[[Category: Rey, F A.]]
-[[Category: Ruemenapf, T.]]
-[[Category: Vaney, M C.]]
-[[Category: Vonrhein, C.]]
-[[Category: T2 ribonuclease]]
-[[Category: Viral protein]]
-[[Category: Virus glycoprotein]]

4dwc

From Proteopedia

Current revision

Crystal structure of the glycoprotein Erns from the pestivirus BVDV-1 in complex with Zn ions

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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