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The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.

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.

SUBMITTER: Volpon L

PROVIDER: S-EPMC164884 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature

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The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.

Volpon Laurent L Lievre Carine C Osborne Michael J MJ Gandhi Shaifali S Iannuzzi Pietro P Larocque Robert R Cygler Miroslaw M Gehring Kalle K Ekiel Irena I

Journal of bacteriology 20030701 14

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 K5 ...[more]

PMID: 12837795

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