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4ZNP

The structure of A pfI Riboswitch Bound to ZMP

Summary for 4ZNP
Entry DOI10.2210/pdb4znp/pdb
DescriptorpfI Riboswitch, AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordszmp, riboswitch, rna, one carbon mechanism, aicar, ztp, complex
Biological sourcesynthetic construct
Total number of polymer chains2
Total formula weight48167.77
Authors
Ren, A.,Patel, D.J.,Rajashankar, R.K. (deposition date: 2015-05-05, release date: 2015-08-26, Last modification date: 2024-03-06)
Primary citationRen, A.,Rajashankar, K.R.,Patel, D.J.
Global RNA Fold and Molecular Recognition for a pfl Riboswitch Bound to ZMP, a Master Regulator of One-Carbon Metabolism.
Structure, 23:1375-1381, 2015
Cited by
PubMed Abstract: ZTP, the pyrophosphorylated analog of ZMP (5-amino-4-imidazole carboxamide ribose-5'-monophosphate), was identified as an alarmone that senses 10-formyl-tetrahydroflate deficiency in bacteria. Recently, a pfl riboswitch was identified that selectively binds ZMP and regulates genes associated with purine biosynthesis and one-carbon metabolism. We report on the structure of the ZMP-bound Thermosinus carboxydivorans pfl riboswitch sensing domain, thereby defining the pseudoknot-based tertiary RNA fold, the binding-pocket architecture, and principles underlying ligand recognition specificity. Molecular recognition involves shape complementarity, with the ZMP 5-amino and carboxamide groups paired with the Watson-Crick edge of an invariant uracil, and the imidazole ring sandwiched between guanines, while the sugar hydroxyls form intermolecular hydrogen bond contacts. The burial of the ZMP base and ribose moieties, together with unanticipated coordination of the carboxamide by Mg(2+), contrasts with exposure of the 5'-phosphate to solvent. Our studies highlight the principles underlying RNA-based recognition of ZMP, a master regulator of one-carbon metabolism.
PubMed: 26118534
DOI: 10.1016/j.str.2015.05.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.94 Å)
Structure validation

226707

건을2024-10-30부터공개중

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