View source for 2jlu


==Dengue virus 4 NS3 helicase in complex with ssRNA==
<StructureSection load='2jlu' size='340' side='right'caption='[[2jlu]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jlu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Den4t Den4t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JLU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jlq|2jlq]], [[2jlr|2jlr]], [[2jls|2jls]], [[2jlv|2jlv]], [[2jlw|2jlw]], [[2jlx|2jlx]], [[2jly|2jly]], [[2jlz|2jlz]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Flavivirin Flavivirin], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2jlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlu OCA], [https://pdbe.org/2jlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jlu RCSB], [https://www.ebi.ac.uk/pdbsum/2jlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jlu ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jl/2jlu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <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/main_output.php?pdb_ID=2jlu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Together 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<ref>PMID:19008861</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jlu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Den4t]]
[[Category: Flavivirin]]
[[Category: Large Structures]]
[[Category: Becker, D S]]
[[Category: Jahnke, W]]
[[Category: Lescar, J]]
[[Category: Lim, S P]]
[[Category: Luo, D H]]
[[Category: Sampath, A]]
[[Category: Vasudevan, S G]]
[[Category: Wang, C H]]
[[Category: Watson, R P]]
[[Category: Xu, T]]
[[Category: Yeong, S S]]
[[Category: Atp-binding]]
[[Category: Atpase]]
[[Category: Capsid protein]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Dengue virus]]
[[Category: Endoplasmic reticulum]]
[[Category: Envelope protein]]
[[Category: Flaviviruse]]
[[Category: Glycoprotein]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Hydrolase-rna complex]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Multifunctional enzyme]]
[[Category: Ns3 helicase structure]]
[[Category: Nucleotide-binding]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protease]]
[[Category: Ribonucleoprotein]]
[[Category: Rna replication]]
[[Category: Rna-binding]]
[[Category: Rna-directed rna polymerase]]
[[Category: Secreted]]
[[Category: Serine protease]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Transmembrane]]
[[Category: Viral nucleoprotein]]
[[Category: Virion]]