1P9K

THE SOLUTION STRUCTURE OF YBCJ FROM E. COLI REVEALS A RECENTLY DISCOVERED ALFAL MOTIF INVOLVED IN RNA-BINDING

Replaces:  1O09

Summary for 1P9K

• Entry DOI: 10.2210/pdb1p9k/pdb
• NMR Information: BMRB: 5818
• Descriptor: orf, hypothetical protein (1 entity in total)
• Functional Keywords: alfal motif, rna-binding protein, e.coli, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, rna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 8416.74

Authors

Volpon, L.,Lievre, C.,Osborne, M.J.,Gandhi, S.,Iannuzzi, P.,Larocque, R.,Matte, A.,Cygler, M.,Gehring, K.,Ekiel, I.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2003-05-12, release date: 2003-11-25, Last modification date: 2024-05-01)

Primary citation

Volpon, L.,Lievre, C.,Osborne, M.J.,Gandhi, S.,Iannuzzi, P.,Larocque, R.,Cygler, M.,Gehring, K.,Ekiel, I.
The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.
J.Bacteriol., 185:4204-4210, 2003

PubMed 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.

PubMed: 12837795
DOI: 10.1128/JB.185.14.4204-4210.2003

Experimental method

SOLUTION NMR