6p78

queuine lyase from Clostridium spiroforme bound to SAM and queuine

spinqualitylabelsall models 6p78, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6p78 is a 1 chain structure with sequence from Clostridium spiroforme DSM 1552. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.726Å Ligands: QUG, SAM, SMC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B1C2R2_9FIRM Publication Abstract from PubMed Queuosine (Q) is a complex tRNA modification widespread in eukaryotes and bacteria that contributes to the efficiency and accuracy of protein synthesis. Eukaryotes are not capable of Q synthesis and rely on salvage of the queuine base (q) as a Q precursor. While many bacteria are capable of Q de novo synthesis, salvage of the prokaryotic Q precursors preQ0 and preQ1 also occurs. With the exception of Escherichia coli YhhQ, shown to transport preQ0 and preQ1, the enzymes and transporters involved in Q salvage and recycling have not been well described. We discovered and characterized 2 Q salvage pathways present in many pathogenic and commensal bacteria. The first, found in the intracellular pathogen Chlamydia trachomatis, uses YhhQ and tRNA guanine transglycosylase (TGT) homologs that have changed substrate specificities to directly salvage q, mimicking the eukaryotic pathway. The second, found in bacteria from the gut flora such as Clostridioides difficile, salvages preQ1 from q through an unprecedented reaction catalyzed by a newly defined subgroup of the radical-SAM enzyme family. The source of q can be external through transport by members of the energy-coupling factor (ECF) family or internal through hydrolysis of Q by a dedicated nucleosidase. This work reinforces the concept that hosts and members of their associated microbiota compete for the salvage of Q precursors micronutrients. Discovery of novel bacterial queuine salvage enzymes and pathways in human pathogens.,Yuan Y, Zallot R, Grove TL, Payan DJ, Martin-Verstraete I, Sepic S, Balamkundu S, Neelakandan R, Gadi VK, Liu CF, Swairjo MA, Dedon PC, Almo SC, Gerlt JA, de Crecy-Lagard V Proc Natl Acad Sci U S A. 2019 Sep 17;116(38):19126-19135. doi:, 10.1073/pnas.1909604116. Epub 2019 Sep 3. PMID:31481610 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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