5af2: Difference between revisions
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==Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3== | ==Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3== | ||
<StructureSection load='5af2' size='340' side='right' caption='[[5af2]], [[Resolution|resolution]] 1.39Å' scene=''> | <StructureSection load='5af2' size='340' side='right'caption='[[5af2]], [[Resolution|resolution]] 1.39Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5af2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AF2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5af2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Group_a_rotaviruses Group a rotaviruses]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AF2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=5af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af2 OCA], [http://pdbe.org/5af2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5af2 RCSB], [http://www.ebi.ac.uk/pdbsum/5af2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5af2 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=5af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af2 OCA], [http://pdbe.org/5af2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5af2 RCSB], [http://www.ebi.ac.uk/pdbsum/5af2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5af2 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Group a rotaviruses]] | |||
[[Category: Large Structures]] | |||
[[Category: Brandmann, T]] | [[Category: Brandmann, T]] | ||
[[Category: Jinek, M]] | [[Category: Jinek, M]] |
Revision as of 10:20, 3 July 2019
Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3
Structural highlights
Publication Abstract from PubMedIn response to viral infections, the mammalian innate immune system induces the production of the second messenger 2'-5' oligoadenylate (2-5A) to activate latent ribonuclease L (RNase L) that restricts viral replication and promotes apoptosis. A subset of rotaviruses and coronaviruses encode 2',5'-phosphodiesterase enzymes that hydrolyze 2-5A, thereby inhibiting RNase L activation. We report the crystal structure of the 2',5'-phosphodiesterase domain of group A rotavirus protein VP3 at 1.39 A resolution. The structure exhibits a 2H phosphoesterase fold and reveals conserved active site residues, providing insights into the mechanism of 2-5A degradation in viral evasion of host innate immunity. This article is protected by copyright. All rights reserved. Crystal structure of the C-terminal 2',5'-phosphodiesterase domain of group A rotavirus protein VP3.,Brandmann T, Jinek M Proteins. 2015 Mar 10. doi: 10.1002/prot.24794. PMID:25758703[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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