2jlq: Difference between revisions
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==Dengue virus 4 NS3 helicase structure, apo enzyme.== | ==Dengue virus 4 NS3 helicase structure, apo enzyme.== | ||
<StructureSection load='2jlq' size='340' side='right' caption='[[2jlq]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='2jlq' size='340' side='right'caption='[[2jlq]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jlq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Den4t Den4t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLQ OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2jlq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Den4t Den4t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JLQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jlr|2jlr]], [[2jls|2jls]], [[2jlu|2jlu]], [[2jlv|2jlv]], [[2jlw|2jlw]], [[2jlx|2jlx]], [[2jly|2jly]], [[2jlz|2jlz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jlr|2jlr]], [[2jls|2jls]], [[2jlu|2jlu]], [[2jlv|2jlv]], [[2jlw|2jlw]], [[2jlx|2jlx]], [[2jly|2jly]], [[2jlz|2jlz]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavivirin Flavivirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.91 3.4.21.91] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavivirin Flavivirin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.91 3.4.21.91] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlq OCA], [http://pdbe.org/2jlq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jlq RCSB], [http://www.ebi.ac.uk/pdbsum/2jlq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jlq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Helicase|Helicase]] | *[[Helicase 3D structures|Helicase 3D structures]] | ||
*[[Virus proteases 3D strutures|Virus proteases 3D strutures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Den4t]] | [[Category: Den4t]] | ||
[[Category: Flavivirin]] | [[Category: Flavivirin]] | ||
[[Category: Large Structures]] | |||
[[Category: Becker, D S]] | [[Category: Becker, D S]] | ||
[[Category: Jahnke, W]] | [[Category: Jahnke, W]] | ||
Revision as of 10:55, 15 April 2020
Dengue virus 4 NS3 helicase structure, apo enzyme.Dengue virus 4 NS3 helicase structure, apo enzyme.
Structural highlights
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 PubMedTogether with the NS5 polymerase, the NS3 helicase has a pivotal function in flavivirus RNA replication and constitutes an important drug target. We captured the dengue virus NS3 helicase at several stages along the catalytic pathway including bound to single-stranded (ss) RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent in a way remarkably similar to eukaryotic DEAD box proteins Vasa and eIF4AIII. On ssRNA binding, the NS3 enzyme switches to a catalytic-competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. These structures demonstrate for the first time large quaternary changes in the flaviviridae helicase, identify the catalytic water molecule and point to a beta-hairpin that protrudes from subdomain 2, as a critical element for dsRNA unwinding. They also suggest how NS3 could exert an effect as an RNA-anchoring device and thus participate both in flavivirus RNA replication and assembly. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein.,Luo D, Xu T, Watson RP, Scherer-Becker D, Sampath A, Jahnke W, Yeong SS, Wang CH, Lim SP, Strongin A, Vasudevan SG, Lescar J EMBO J. 2008 Dec 3;27(23):3209-19. Epub 2008 Nov 13. PMID:19008861[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Den4t
- Flavivirin
- Large Structures
- Becker, D S
- Jahnke, W
- Lescar, J
- Lim, S P
- Luo, D H
- Sampath, A
- Vasudevan, S G
- Wang, C H
- Watson, R P
- Xu, T
- Yeong, S S
- Atp-binding
- Atpase
- Capsid protein
- Cleavage on pair of basic residue
- Dengue virus
- Endoplasmic reticulum
- Envelope protein
- Flaviviruse
- Glycoprotein
- Helicase
- Hydrolase
- Membrane
- Metal-binding
- Multifunctional enzyme
- Ns3 helicase structure
- Nucleotide-binding
- Nucleotidyltransferase
- Nucleus
- Phosphoprotein
- Protease
- Ribonucleoprotein
- Rna replication
- Rna-binding
- Rna-directed rna polymerase
- Secreted
- Serine protease
- Transcription
- Transcription regulation
- Transferase
- Transmembrane
- Viral nucleoprotein
- Virion