View source for 4pjr


==Crystal structure of designed cPPR-NRE protein==
<StructureSection load='4pjr' size='340' side='right'caption='[[4pjr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pjr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PJR 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4pjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pjr OCA], [https://pdbe.org/4pjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pjr RCSB], [https://www.ebi.ac.uk/pdbsum/4pjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pjr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pentatricopeptide repeat (PPR) proteins control diverse aspects of RNA metabolism in eukaryotic cells. Although recent computational and structural studies have provided insights into RNA recognition by PPR proteins, their highly insoluble nature and inconsistencies between predicted and observed modes of RNA binding have restricted our understanding of their biological functions and their use as tools. Here we use a consensus design strategy to create artificial PPR domains that are structurally robust and can be programmed for sequence-specific RNA binding. The atomic structures of these artificial PPR domains elucidate the structural basis for their stability and modelling of RNA-protein interactions provides mechanistic insights into the importance of RNA-binding residues and suggests modes of PPR-RNA association. The modular mode of RNA binding by PPR proteins holds great promise for the engineering of new tools to target RNA and to understand the mechanisms of gene regulation by natural PPR proteins.

An artificial PPR scaffold for programmable RNA recognition.,Coquille S, Filipovska A, Chia T, Rajappa L, Lingford JP, Razif MF, Thore S, Rackham O Nat Commun. 2014 Dec 17;5:5729. doi: 10.1038/ncomms6729. PMID:25517350<ref>PMID:25517350</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pjr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Unidentified]]
[[Category: Chia TS]]
[[Category: Coquille SC]]
[[Category: Filipovska A]]
[[Category: Lingford JP]]
[[Category: Rackham O]]
[[Category: Rajappa L]]
[[Category: Razif MFM]]
[[Category: Thore S]]