6dlx

FtsY-NG domain bound to fragment 3.

spinqualitylabelsall models 6dlx, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dlx is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.848Å Ligands: GXY, NH4, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSY_ECOLI Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Signal recognition particle receptor

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