2jlv: Difference between revisions

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[[Image:2jlv.png|left|200px]]
==DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND AMPPNP==
<StructureSection load='2jlv' size='340' side='right' caption='[[2jlv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jlv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_4 Dengue virus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JLV FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jlr|2jlr]], [[2jlq|2jlq]], [[2jlx|2jlx]], [[2jlu|2jlu]], [[2jls|2jls]], [[2jlz|2jlz]], [[2jly|2jly]], [[2jlw|2jlw]]</td></tr>
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jlv RCSB], [http://www.ebi.ac.uk/pdbsum/2jlv PDBsum]</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/2jlv_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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_2jlv|  PDB=2jlv  |  SCENE=  }}
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>


===DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND AMPPNP===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_19008861}}
 
==About this Structure==
[[2jlv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_4 Dengue virus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLV OCA].


==See Also==
==See Also==
*[[Helicase|Helicase]]
*[[Helicase|Helicase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019008861</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Dengue virus 4]]
[[Category: Dengue virus 4]]
[[Category: Flavivirin]]
[[Category: Flavivirin]]

Revision as of 05:14, 29 September 2014

DENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND AMPPNPDENGUE VIRUS 4 NS3 HELICASE IN COMPLEX WITH SSRNA AND AMPPNP

Structural highlights

2jlv is a 4 chain structure with sequence from Dengue virus 4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Related:2jlr, 2jlq, 2jlx, 2jlu, 2jls, 2jlz, 2jly, 2jlw
Activity:Flavivirin, with EC number 3.4.21.91
Resources:FirstGlance, OCA, RCSB, PDBsum

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 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[1]

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

See Also

References

  1. ↑ 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. Insights into RNA unwinding and ATP hydrolysis by the flavivirus NS3 protein. EMBO J. 2008 Dec 3;27(23):3209-19. Epub 2008 Nov 13. PMID:19008861 doi:10.1038/emboj.2008.232

2jlv, resolution 1.90Å

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