6dlx

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'''Unreleased structure'''
 
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The entry 6dlx is ON HOLD until Paper Publication
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==FtsY-NG domain bound to fragment 3.==
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<StructureSection load='6dlx' size='340' side='right' caption='[[6dlx]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6dlx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DLX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DLX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GXY:4-bromo-2,5-dimethoxyaniline'>GXY</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<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=6dlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dlx OCA], [http://pdbe.org/6dlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dlx RCSB], [http://www.ebi.ac.uk/pdbsum/6dlx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dlx ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Given the increasing incidence of antibiotic resistance, antibiotics that employ new strategies are urgently needed. Bacterial survival is dependent on proper function of the signal recognition particle (SRP) and its receptor (FtsY). A unique set of interactions in FtsY:SRP-RNA represents a promising candidate for new antibiotic development as no antibiotic targets this complex and these interactions are functionally replaced by protein:protein interactions in eukaryotes. We used a Fragment Based Drug Design (FBDD) approach to search for new compounds that can bind FtsY, and have identified three lead fragments. In vitro and in vivo analyses have shown that despite a high micromolar binding affinity, one fragment has some antimicrobial properties. X-ray structures of E. coli FtsY:fragments reveal the fragments bind in the targeted RNA interaction site. Our results show that FBDD is a suitable approach for targeting FtsY:SRP-RNA for antibiotic development and opens the possibility of targeting protein:RNA interactions in general.
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Authors: Ataide, F.S., Faoro, C.
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Discovery of fragments that target key interactions in the signal recognition particle (SRP) as potential leads for a new class of antibiotics.,Faoro C, Wilkinson-White L, Kwan AH, Ataide SF PLoS One. 2018 Jul 25;13(7):e0200387. doi: 10.1371/journal.pone.0200387., eCollection 2018. PMID:30044812<ref>PMID:30044812</ref>
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Description: FtsY-NG domain bound to fragment 3.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6dlx" style="background-color:#fffaf0;"></div>
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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: Ataide, F S]]
[[Category: Faoro, C]]
[[Category: Faoro, C]]
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[[Category: Ataide, F.S]]
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[[Category: Fbdd]]
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[[Category: Ftsy]]
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[[Category: Signaling protein]]
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[[Category: Sr receptor]]
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[[Category: Srp]]

Revision as of 06:08, 22 August 2018

FtsY-NG domain bound to fragment 3.

6dlx, resolution 1.85Å

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