来自大肠杆菌的YbcJ的溶液结构揭示了一个最近发现的参与RNA结合的αL基序。
The solution structure of YbcJ from Escherichia coli reveals a recently discovered alphaL motif involved in RNA binding.
作者信息
Volpon Laurent, Lievre Carine, Osborne Michael J, Gandhi Shaifali, Iannuzzi Pietro, Larocque Robert, Cygler Miroslaw, Gehring Kalle, Ekiel Irena
机构信息
Department of Biochemistry, McGill University, Montreal, Quebec, H3G 1Y6, Canada.
出版信息
J Bacteriol. 2003 Jul;185(14):4204-10. doi: 10.1128/JB.185.14.4204-4210.2003.
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.
摘要
通过核磁共振确定了重组大肠杆菌蛋白YbcJ的结构，它是细菌蛋白保守家族（COG2501）的代表。YbcJ的折叠结构表明它是更大的S4样RNA结合结构域家族的成员。这些结构域与结构化RNA结合，如tRNA、rRNA和mRNA假结中的RNA。YbcJ的结构揭示了一个高度保守的碱性残基区域，包括氨基酸K26、K38、R55、K56和K59，它们可能参与RNA结合。
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