6OD9

Co-crystal structure of the Fusobacterium ulcerans ZTP riboswitch using an X-ray free-electron laser

Summary for 6OD9

• Entry DOI: 10.2210/pdb6od9/pdb
• Related: 5BTP
• Descriptor: RNA (75-MER), MAGNESIUM ION, AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: complex, riboswitch, x-ray free-electron diffraction, xfel, zmp, ztp, rna
• Biological source: Fusobacterium ulcerans
• Total number of polymer chains: 2
• Total formula weight: 49581.20

Authors

Jones, C.P.,Tran, B.,Ferre-D'Amare, A.R. (deposition date: 2019-03-26, release date: 2019-07-17, Last modification date: 2023-10-11)

Primary citation

Jones, C.,Tran, B.,Conrad, C.,Stagno, J.,Trachman 3rd, R.,Fischer, P.,Meents, A.,Ferre-D'Amare, A.
Co-crystal structure of the Fusobacterium ulcerans ZTP riboswitch using an X-ray free-electron laser.
Acta Crystallogr.,Sect.F, 75:496-500, 2019

PubMed Abstract: Riboswitches 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 Å resolution. This model, which was refined against a data set from ∼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.

PubMed: 31282869
DOI: 10.1107/S2053230X19008549

Experimental method

X-RAY DIFFRACTION (4.102 Å)