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The Solution Structure of YbcJ from Escherichia coli Reveals a Recently Discovered L Motif Involved in RNA Binding

Department of Biochemistry, McGill University, Montreal, Quebec, H3G 1Y6,¹ NMR Group, Biotechnology Research Institute, National Research Council of Canada,² Macromolecular Structure Group, Biotechnology Research Institute, Montreal, Quebec, H4P 2R2,³ Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, H3G 1M8, Canada⁴

Received 7 February 2003/ Accepted 25 April 2003

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.

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