5e6f: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='5e6f' size='340' side='right' caption='[[5e6f]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5e6f' size='340' side='right' caption='[[5e6f]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e6f]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6F FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e6f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Avipoxvirus_clade_b1 Avipoxvirus clade b1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E6F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=5e6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6f OCA], [http://pdbe.org/5e6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6f RCSB], [http://www.ebi.ac.uk/pdbsum/5e6f PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CNPV261 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44088 Avipoxvirus clade B1])</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=5e6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e6f OCA], [http://pdbe.org/5e6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e6f RCSB], [http://www.ebi.ac.uk/pdbsum/5e6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e6f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 20: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Avipoxvirus clade b1]] | |||
[[Category: Bushman, F D]] | [[Category: Bushman, F D]] | ||
[[Category: Duyne, G D.Van]] | [[Category: Duyne, G D.Van]] | ||
Revision as of 15:36, 6 November 2017
Canarypox virus resolvaseCanarypox virus resolvase
Structural highlights
Publication Abstract from PubMedPoxviruses replicate their linear genomes by forming concatemers that must be resolved into monomeric units in order to produce new virions. A viral resolvase cleaves DNA 4-way junctions extruded at the concatemer junctions to produce monomeric genomes. This cleavage reaction is required for viral replication, so the resolvase is an attractive target for small molecule inhibitors. To provide a platform for understanding resolvase mechanism and designing inhibitors, we have determined the crystal structure of the canarypox virus (CPV) resolvase. CPV resolvase is dimer of RNase H superfamily domains related to E. coli RuvC, with an active site lined by highly conserved, acidic residues that bind metal ions. There are several intriguing structural differences between resolvase and RuvC and a model of the CPV resolvase.HJ complex provides insights into the consequences of these differences, including a plausible explanation for the weak sequence specificity exhibited by the poxvirus enzymes. The model also explains why the poxvirus resolvases are more promiscuous than RuvC, cleaving a variety of branched, bulged, and flap containing substrates. Based on the unique active site structure observed for CPV resolvase, we have carried out a series of experiments to test divalent ion usage and preferences. We find that the two resolvase metal binding sites have different preferences for Mg2+vs. Mn2+ Optimal resolvase activity is maintained with 5 muM Mn2+and 100 muM Mg2+, concentrations that are well below those required for either metal alone. Together, our findings provide biochemical insights and structural models that will facilitate studying poxvirus replication and the search for efficient poxvirus inhibitors. Structure and metal-binding properties of a poxvirus resolvase.,Li H, Hwang Y, Perry K, Bushman F, Van Duyne GD J Biol Chem. 2016 Mar 24. pii: jbc.M115.709139. PMID:27013661[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||