Publication Abstract from PubMed
E. coli YhbY belongs to a conserved family of hypothetical proteins represented in eubacteria, archaea, and plants (Pfam code UPF0044). Three maize proteins harboring UPF0044-like domains are required for chloroplast group II intron splicing, and bioinformatic data suggest a role for prokaryotic UPF0044 members in translation. The crystal structure of YhbY has been determined. YhbY has a fold similar to that of the C-terminal domain of translation initiation factor 3 (IF3C), which binds to 16S rRNA in the 30S ribosome. Modeling studies indicate that the same surface is highly basic in all members of UPF0044, suggesting a conserved RNA binding surface. Taken together, the evidence suggests that members of UPF0044 constitute a previously unrecognized class of RNA binding domain.
Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins.,Ostheimer GJ, Barkan A, Matthews BW Structure. 2002 Nov;10(11):1593-601. PMID:12429100[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
