Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

被引：9
|
作者：
Wang, HF
Takemoto, CH
Murayama, K
Sakai, H
Tatsuguchi, A
Terada, T
Shirouzu, M
Kuramitsu, S
Yokoyama, S
机构：
[1] RIKEN, Genomic Sci Ctr, Prot Res Grp, Yokohama, Kanagawa 2300045, Japan
[2] Osaka Univ, Grad Sch Sci, Dept Biol, Osaka 5600043, Japan
[3] Univ Tokyo, Grad Sch Sci, Dept Biochem & Biophys, Tokyo 1130033, Japan
来源：
PROTEIN SCIENCE | 2004年 / 13卷 / 10期
关键词：
ribosomal protein L27; protein-RNA interactions; ribosome; Thermus thermophilus HB8; crystal structure;
D O I：
10.1110/ps.04864904
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Ribosomal protein L27 is located near the peptidyltransferase center at the interface of ribosomal subunits, and is important for ribosomal assembly and function. We report the crystal structure of ribosomal protein L27 from Thermus thermophilus HB8, which was determined by the multiwavelength anomalous dispersion method and refined to an R-factor of 19.7% (R-free = 23.6%) at 2.8 Angstrom resolution. The overall fold is an all beta-sheet hybrid. It consists of two sets of four-stranded beta-sheets formed around a well-defined hydrophobic core, with a highly positive charge on the protein surface. The structure of ribosomal protein L27 from T. thermophilus HB8 in the RNA-free form is investigated, and its functional roles in the ribosomal subunit are discussed.
引用
收藏
页码：2806 / 2810
页数：5
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