2bhr
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2bhr.png|left|200px]] | ||
- | < | + | ==Dengue virus RNA helicase== |
- | + | <StructureSection load='2bhr' size='340' side='right'caption='[[2bhr]], [[Resolution|resolution]] 2.80Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[2bhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHR FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2bhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhr OCA], [https://pdbe.org/2bhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhr RCSB], [https://www.ebi.ac.uk/pdbsum/2bhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhr ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q91H74_9FLAV Q91H74_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS026470_004_099774] | ||
+ | == 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/bh/2bhr_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=2bhr ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Dengue fever is an important emerging public health concern, with several million viral infections occurring annually, for which no effective therapy currently exists. The NS3 protein from Dengue virus is a multifunctional protein of 69 kDa, endowed with protease, helicase, and nucleoside 5'-triphosphatase (NTPase) activities. Thus, NS3 plays an important role in viral replication and represents a very interesting target for the development of specific antiviral inhibitors. We present the structure of an enzymatically active fragment of the Dengue virus NTPase/helicase catalytic domain to 2.4 A resolution. The structure is composed of three domains, displays an asymmetric distribution of charges on its surface, and contains a tunnel large enough to accommodate single-stranded RNA. Its C-terminal domain adopts a new fold compared to the NS3 helicase of hepatitis C virus, which has interesting implications for the evolution of the Flaviviridae replication complex. A bound sulfate ion reveals residues involved in the metal-dependent NTPase catalytic mechanism. Comparison with the NS3 hepatitis C virus helicase complexed to single-stranded DNA would place the 3' single-stranded tail of a nucleic acid duplex in the tunnel that runs across the basic face of the protein. A possible model for the unwinding mechanism is proposed. | ||
- | + | Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A.,Xu T, Sampath A, Chao A, Wen D, Nanao M, Chene P, Vasudevan SG, Lescar J J Virol. 2005 Aug;79(16):10278-88. PMID:16051821<ref>PMID:16051821</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2bhr" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Helicase 3D structures|Helicase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
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- | == | + | |
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[[Category: Dengue virus 2]] | [[Category: Dengue virus 2]] | ||
- | [[Category: Chao | + | [[Category: Large Structures]] |
- | [[Category: Chene | + | [[Category: Chao A]] |
- | [[Category: Lescar | + | [[Category: Chene P]] |
- | [[Category: Nanao | + | [[Category: Lescar J]] |
- | [[Category: Sampath | + | [[Category: Nanao M]] |
- | [[Category: Vasudevan | + | [[Category: Sampath A]] |
- | [[Category: Wen | + | [[Category: Vasudevan SG]] |
- | [[Category: Xu | + | [[Category: Wen D]] |
- | + | [[Category: Xu T]] | |
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Current revision
Dengue virus RNA helicase
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Categories: Dengue virus 2 | Large Structures | Chao A | Chene P | Lescar J | Nanao M | Sampath A | Vasudevan SG | Wen D | Xu T