5orm
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of designed cPPR-Telo1== | |
+ | <StructureSection load='5orm' size='340' side='right' caption='[[5orm]], [[Resolution|resolution]] 2.08Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5orm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ORM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ORM FirstGlance]. <br> | ||
+ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5orm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5orm OCA], [http://pdbe.org/5orm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5orm RCSB], [http://www.ebi.ac.uk/pdbsum/5orm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5orm ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | DNA is typically found as a double helix, however it must be separated into single strands during all phases of DNA metabolism; including transcription, replication, recombination and repair. Although recent breakthroughs have enabled the design of modular RNA- and double-stranded DNA-binding proteins, there are currently no tools available to manipulate single-stranded DNA (ssDNA). Here we show that artificial pentatricopeptide repeat (PPR) proteins can be programmed for sequence-specific ssDNA binding. Interactions occur using the same code and specificity as for RNA binding. We solve the structures of DNA-bound and apo proteins revealing the basis for ssDNA binding and how hydrogen bond rearrangements enable the PPR structure to envelope its ssDNA target. Finally, we show that engineered PPRs can be designed to bind telomeric ssDNA and can block telomerase activity. The modular mode of ssDNA binding by PPR proteins provides tools to target ssDNA and to understand its importance in cells. | ||
- | + | Modular ssDNA binding and inhibition of telomerase activity by designer PPR proteins.,Spahr H, Chia T, Lingford JP, Siira SJ, Cohen SB, Filipovska A, Rackham O Nat Commun. 2018 Jun 7;9(1):2212. doi: 10.1038/s41467-018-04388-1. PMID:29880855<ref>PMID:29880855</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5orm" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Rackham, O]] | ||
+ | [[Category: Spahr, H]] | ||
+ | [[Category: De novo protein]] | ||
+ | [[Category: Designer nucleic acid-binding protein]] | ||
+ | [[Category: Pentatricopeptide repeat]] | ||
+ | [[Category: Telomerase]] |
Revision as of 05:38, 20 June 2018
Crystal structure of designed cPPR-Telo1
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