PMID:12837795

Citation	Volpon, L, Lievre, C, Osborne, MJ, Gandhi, S, Iannuzzi, P, Larocque, R, Cygler, M, Gehring, K and Ekiel, I (2003) The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding. J. Bacteriol. 185:4204-10
Abstract	The structure of the recombinant Escherichia coli protein YbcJ, a representative of a conserved family of bacterial proteins (COG2501), was determined by nuclear magnetic resonance. The fold of YbcJ identified it as a member of the larger family of S4-like RNA binding domains. These domains bind to structured RNA, such as that found in tRNA, rRNA, and a pseudoknot of mRNA. The structure of YbcJ revealed a highly conserved patch of basic residues, comprising amino acids K26, K38, R55, K56, and K59, which likely participate in RNA binding.
Links	PubMed PMC164884
Keywords	Amino Acid Motifs; Amino Acid Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; RNA, Bacterial/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Recombinant Proteins/chemistry; Solutions
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