Structural highlights
Function
[YBCJ_ECOLI] Its structure and the presence of conserved basic residues indicates that it probably binds RNA.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.,Volpon L, Lievre C, Osborne MJ, Gandhi S, Iannuzzi P, Larocque R, Cygler M, Gehring K, Ekiel I J Bacteriol. 2003 Jul;185(14):4204-10. PMID:12837795[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Volpon L, Lievre C, Osborne MJ, 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. 2003 Jul;185(14):4204-10. PMID:12837795
