7mgt

Ftp from Treponema pallidum bound to an ADP-like inhibitor

spinqualitylabelsall models 7mgt, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mgt is a 1 chain structure with sequence from Treponema pallidum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Ligands: EDO, MG, ZD4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APBE_TREPA Involved in the conversion of aminoimidazole ribotide (AIR), a purine intermediate, to the 4-amino-5-hydroxymethyl-2-methyl pyrimidine (HMP) moiety of thiamine (By similarity). Publication Abstract from PubMed Antibiotic resistance is a challenge for the control of bacterial infections. In an effort to explore unconventional avenues for antibacterial drug development, we focused on the FMN-transferase activity of the enzyme Ftp from the syphilis spirochete, Treponema pallidum (Ftp_Tp). This enzyme, which is only found in prokaryotes and trypanosomatids, post-translationally modifies proteins in the periplasm, covalently linking FMN (from FAD) to proteins that typically are important for establishing an essential electrochemical gradient across the cytoplasmic membrane. As such, Ftp inhibitors potentially represent a new class of antimicrobials. Previously, we showed that AMP is both a product of the Ftp_tp-catalyzed reaction and an inhibitor of the enzyme. As a preliminary step in exploiting this property to develop a novel Ftp_Tp inhibitor, we have used structural and solution studies to examine the inhibitory and enzyme-binding properties of several adenine-based nucleosides, with particular focus on the 2-position of the purine ring. Implications for future drug design are discussed. Inhibition of bacterial FMN transferase: A potential avenue for countering antimicrobial resistance.,Deka RK, Deka A, Liu WZ, Norgard MV, Brautigam CA Protein Sci. 2021 Nov 19. doi: 10.1002/pro.4241. PMID:34796555 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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