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5VJB

Guanidine-II riboswitch P2 hairpin dimer with 5-bromoU substitution from Pseudomonas aeruginosa

Summary for 5VJB
Entry DOI10.2210/pdb5vjb/pdb
Related5VJ9
DescriptorRNA (5'-R(*GP*CP*GP*GP*GP*GP*AP*CP*GP*AP*CP*CP*CP*(5BU)P*GP*C)-3'), GUANIDINE, SPERMINE, ... (5 entities in total)
Functional Keywordsguanidine, riboswitch, kissing loop, hairpin, rna
Biological sourcePseudomonas aeruginosa
Total number of polymer chains4
Total formula weight22054.13
Authors
Reiss, C.W.,Strobel, S.A. (deposition date: 2017-04-19, release date: 2017-06-28, Last modification date: 2024-03-13)
Primary citationReiss, C.W.,Strobel, S.A.
Structural basis for ligand binding to the guanidine-II riboswitch.
RNA, 23:1338-1343, 2017
Cited by
PubMed Abstract: The guanidine-II riboswitch, also known as , is a conserved mRNA element with more than 800 examples in bacteria. It consists of two stem-loops capped by identical, conserved tetraloops that are separated by a linker region of variable length and sequence. Like the guanidine-I riboswitch, it controls the expression of guanidine carboxylases and SugE-like genes. The guanidine-II riboswitch specifically binds free guanidinium cations and functions as a translationally controlled on-switch. Here we report the structure of a P2 stem-loop from the guanidine-II riboswitch aptamer bound to guanidine at 1.57 Å resolution. The hairpins dimerize via the conserved tetraloop, which also contains the binding pocket. Two guanidinium molecules bind near the dimerization interface, one in each tetraloop. The guanidinium cation is engaged in extensive hydrogen bonding to the RNA. Contacts include the Hoogsteen face of a guanine base and three nonbridging phosphate oxygens. Cation-π interactions and ionic interactions also stabilize ligand binding. The guanidine-II riboswitch utilizes the same recognition strategies as the guanidine-I riboswitch while adopting an entirely different and much smaller RNA fold.
PubMed: 28600356
DOI: 10.1261/rna.061804.117
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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