PMID:12429100

Citation	Ostheimer, GJ, Barkan, A and Matthews, BW (2002) Crystal structure of E. coli YhbY: a representative of a novel class of RNA binding proteins. Structure 10:1593-601
Abstract	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.
Links	PubMed
Keywords	Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Introns; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Tertiary; RNA/metabolism; RNA, Ribosomal, 16S/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Ribosomes/metabolism; Sequence Homology, Amino Acid
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