4PNO

Escherichia coli Hfq-RNA complex at 0.97 A Resolution

Summary for 4PNO

Entry DOI	10.2210/pdb4pno/pdb
Descriptor	RNA-binding protein Hfq, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
Functional Keywords	rna chaperone hfq rna lsm, rna binding protein
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	8453.62
Authors	Schulz, E.C.,Barabas, O. (deposition date: 2014-05-24, release date: 2014-11-19, Last modification date: 2023-09-27)
Primary citation	Schulz, E.C.,Barabas, O. Structure of an Escherichia coli Hfq:RNA complex at 0.97 angstrom resolution. Acta Crystallogr.,Sect.F, 70:1492-1497, 2014 Cited by PubMed Abstract: In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq-RNA interaction in exceptional detail. PubMed: 25372815 DOI: 10.1107/S2053230X14020044 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (0.97 Å)

Structure validation