2bmf

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[[Image:2bmf.gif|left|200px]]
 
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{{Structure
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==Dengue virus RNA helicase at 2.4A==
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|PDB= 2bmf |SIZE=350|CAPTION= <scene name='initialview01'>2bmf</scene>, resolution 2.41&Aring;
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<StructureSection load='2bmf' size='340' side='right'caption='[[2bmf]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2bmf]] 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=2BMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BMF FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmf OCA], [https://pdbe.org/2bmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmf RCSB], [https://www.ebi.ac.uk/pdbsum/2bmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmf ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmf OCA], [http://www.ebi.ac.uk/pdbsum/2bmf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bmf RCSB]</span>
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[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]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/2bmf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bmf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''DENGUE VIRUS RNA HELICASE AT 2.4A'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bmf" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2BMF is a [[Single protein]] structure of sequence from [http://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=2BMF OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16051821 16051821]
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[[Category: Dengue virus 2]]
[[Category: Dengue virus 2]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chao, A.]]
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[[Category: Chao A]]
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[[Category: Chene, P.]]
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[[Category: Chene P]]
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[[Category: Lescar, J.]]
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[[Category: Lescar J]]
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[[Category: Nanao, M.]]
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[[Category: Nanao M]]
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[[Category: Sampath, A.]]
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[[Category: Sampath A]]
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[[Category: Vasudevan, S G.]]
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[[Category: Vasudevan SG]]
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[[Category: Wen, D.]]
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[[Category: Wen D]]
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[[Category: Xu, T.]]
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[[Category: Xu T]]
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[[Category: dengue virus]]
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[[Category: nucleoside triphosphatase]]
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[[Category: rna helicase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:36 2008''
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Current revision

Dengue virus RNA helicase at 2.4A

PDB ID 2bmf

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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