5fgo: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 5fgo is ON HOLD
+==Crystal structure of D. melanogaster Pur-alpha repeat III.==
+<StructureSection load='5fgo' size='340' side='right'caption='[[5fgo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5fgo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FGO 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]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5fgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fgo OCA], [https://pdbe.org/5fgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fgo RCSB], [https://www.ebi.ac.uk/pdbsum/5fgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fgo ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q95RR6_DROME Q95RR6_DROME]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The neuronal DNA-/RNA-binding protein Pur-alpha is a transcription regulator and core factor for mRNA-localization. Pur-alpha deficient mice die after birth with pleiotropic neuronal defects. Here we report the crystal structure of the DNA-/RNA-binding domain of Pur-alpha in complex with ssDNA. It reveals base-specific recognition and offers a molecular explanation for the effect of point mutations in the 5q31.3 microdeletion syndrome. Consistent with the crystal structure, biochemical and NMR data indicate that Pur-alpha binds DNA and RNA in the same way, suggesting binding modes for tri- and hexanucleotide repeat RNAs in two neurodegenerative RNAopathies. Additionally, structure-based in vitro experiments resolved the molecular mechanism of Pur-alpha's unwindase activity. Complementing in vivo analyses in Drosophila demonstrated the importance of a highly conserved phenylalanine for Pur-alpha's unwinding and neuroprotective function. By uncovering the molecular mechanisms of nucleic-acid binding, this study contributes to understanding the cellular role of Pur-alpha and its implications in neurodegenerative diseases.
-Authors: Windhager, A., Janowski, R., Niessing, D.
+Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alpha.,Weber J, Bao H, Hartlmuller C, Wang Z, Windhager A, Janowski R, Madl T, Jin P, Niessing D Elife. 2016 Jan 8;5. pii: e11297. doi: 10.7554/eLife.11297. PMID:26744780<ref>PMID:26744780</ref>
-Description: Crystal structure of D. melanogaster Pur-alpha repeat III.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Windhager, A]]
+<div class="pdbe-citations 5fgo" style="background-color:#fffaf0;"></div>
-[[Category: Niessing, D]]
+== References ==
-[[Category: Janowski, R]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Drosophila melanogaster]]
+[[Category: Large Structures]]
+[[Category: Janowski R]]
+[[Category: Niessing D]]
+[[Category: Windhager A]]