3gfp

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{{STRUCTURE_3gfp| PDB=3gfp | SCENE= }}
 
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===Structure of the C-terminal domain of the DEAD-box protein Dbp5===
 
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{{ABSTRACT_PUBMED_19805289}}
 
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==About this Structure==
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==Structure of the C-terminal domain of the DEAD-box protein Dbp5==
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[[3gfp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GFP OCA].
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<StructureSection load='3gfp' size='340' side='right'caption='[[3gfp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3gfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GFP FirstGlance]. <br>
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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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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=3gfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gfp OCA], [https://pdbe.org/3gfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gfp RCSB], [https://www.ebi.ac.uk/pdbsum/3gfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gfp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DBP5_YEAST DBP5_YEAST] ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.<ref>PMID:9564047</ref> <ref>PMID:9564048</ref> <ref>PMID:10428971</ref> <ref>PMID:10610322</ref> <ref>PMID:10523319</ref> <ref>PMID:11350039</ref> <ref>PMID:12192043</ref> <ref>PMID:12686617</ref> <ref>PMID:15280434</ref> <ref>PMID:15574330</ref> <ref>PMID:15619606</ref>
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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/gf/3gfp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3gfp 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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The DExD/H-box RNA-dependent ATPase Dbp5 plays an essential role in the nuclear export of mRNA. Dbp5 localizes to the nuclear pore complex, where its ATPase activity is stimulated by Gle1 and its coactivator inositol hexakisphosphate. Here, we present the crystal structure of the C-terminal domain of Dbp5, refined to 1.8 A. The structure reveals a RecA-like fold that contains two defining characteristics not present in other structurally characterized DExD/H-box proteins: a C-terminal alpha-helix and a loop connecting beta5 and alpha4, both of which are composed of conserved and unique elements in the Dbp5 primary sequence. Using structure-guided mutagenesis, we have identified several charged surface residues that, when mutated, weaken the binding of Gle1 and inhibit the ability of Gle1 to stimulate Dbp5's ATPase activity. In vivo analysis of the same mutations reveals that those mutants displaying the weakest ATPase stimulation in vitro are also unable to support yeast growth. Analysis of the correlation between the in vitro and in vivo data indicates that a threshold level of Dbp5 ATPase activity is required for cellular mRNA export that is not met by the unstimulated enzyme, suggesting a possible mechanism by which Dbp5's activity can be modulated to regulate mRNA export.
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==See Also==
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Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.,Dossani ZY, Weirich CS, Erzberger JP, Berger JM, Weis K Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16251-6. Epub 2009 Sep 2. PMID:19805289<ref>PMID:19805289</ref>
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*[[C-terminal domain of the DEAD-box protein Dbp5|C-terminal domain of the DEAD-box protein Dbp5]]
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*[[Helicase|Helicase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:019805289</ref><references group="xtra"/>
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</div>
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<div class="pdbe-citations 3gfp" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Berger, J M.]]
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[[Category: Berger JM]]
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[[Category: Dossani, Z Y.]]
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[[Category: Dossani ZY]]
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[[Category: Erzberger, J P.]]
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[[Category: Erzberger JP]]
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[[Category: Weirich, C S.]]
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[[Category: Weirich CS]]
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[[Category: Weis, K.]]
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[[Category: Weis K]]
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[[Category: Atp-binding]]
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[[Category: Atpase]]
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[[Category: Helicase]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Mrna export]]
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[[Category: Mrna transport]]
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[[Category: Nuclear pore complex]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Protein transport]]
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[[Category: Reca-fold]]
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[[Category: Rna-binding]]
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[[Category: Translocation]]
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[[Category: Transport]]
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Current revision

Structure of the C-terminal domain of the DEAD-box protein Dbp5

PDB ID 3gfp

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