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Co-crystal structure of the Fusobacterium ulcerans ZTP riboswitch using an X-ray free-electron laserCo-crystal structure of the Fusobacterium ulcerans ZTP riboswitch using an X-ray free-electron laser
Structural highlights
Publication Abstract from PubMedRiboswitches are conformationally dynamic RNAs that regulate gene expression by binding specific small molecules. ZTP riboswitches bind the purine-biosynthetic intermediate 5-aminoimidazole-4-carboxamide riboside 5'-monophosphate (ZMP) and its triphosphorylated form (ZTP). Ligand binding to this riboswitch ultimately upregulates genes involved in folate and purine metabolism. Using an X-ray free-electron laser (XFEL), the room-temperature structure of the Fusobacterium ulcerans ZTP riboswitch bound to ZMP has now been determined at 4.1 A resolution. This model, which was refined against a data set from approximately 750 diffraction images (each from a single crystal), was found to be consistent with that previously obtained from data collected at 100 K using conventional synchrotron X-radiation. These experiments demonstrate the feasibility of time-resolved XFEL experiments to understand how the ZTP riboswitch accommodates cognate ligand binding. Co-crystal structure of the Fusobacterium ulcerans ZTP riboswitch using an X-ray free-electron laser.,Jones C, Tran B, Conrad C, Stagno J, Trachman R 3rd, Fischer P, Meents A, Ferre-D'Amare A Acta Crystallogr F Struct Biol Commun. 2019 Jul 1;75(Pt 7):496-500. doi:, 10.1107/S2053230X19008549. Epub 2019 Jun 28. PMID:31282869[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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