Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3OXB

Crystal structure of glycine riboswitch with single mutation

Summary for 3OXB
Entry DOI10.2210/pdb3oxb/pdb
Related3OWI
DescriptorDomain II of glycine riboswitch, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsgene expression regulator, glycine riboswitch, rna
Total number of polymer chains2
Total formula weight58068.77
Authors
Huang, L.,Serganov, A.,Patel, D.J. (deposition date: 2010-09-21, release date: 2010-12-29, Last modification date: 2023-09-06)
Primary citationHuang, L.,Serganov, A.,Patel, D.J.
Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch.
Mol.Cell, 40:774-786, 2010
Cited by
PubMed Abstract: Glycine riboswitches regulate gene expression by feedback modulation in response to cooperative binding to glycine. Here, we report on crystal structures of the second glycine-sensing domain from the Vibrio cholerae riboswitch in the ligand-bound and unbound states. This domain adopts a three-helical fold that centers on a three-way junction and accommodates glycine within a bulge-containing binding pocket above the junction. Glycine recognition is facilitated by a pair of bound Mg(2+) cations and governed by specific interactions and shape complementarity with the pocket. A conserved adenine extrudes from the binding pocket and intercalates into the junction implying that glycine binding in the context of the complete riboswitch could impact on gene expression by stabilizing the riboswitch junction and regulatory P1 helix. Analysis of riboswitch interactions in the crystal and footprinting experiments indicates that adjacent glycine-sensing modules of the riboswitch could form specific interdomain interactions, thereby potentially contributing to the cooperative response.
PubMed: 21145485
DOI: 10.1016/j.molcel.2010.11.026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.947 Å)
Structure validation

227344

數據於2024-11-13公開中

PDB statisticsPDBj update infoContact PDBjnumon