Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

Hongfei Wang, Chie Hori Takemoto, Kazutaka Murayama, Hiroaki Sakai, Ayako Tatsuguchi, Takaho Terada, Mikako Shirouzu, Seiki Kuramitsu, Shigeyuki Yokoyama

研究成果: Article査読

10 被引用数 (Scopus)

抄録

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% (Rfree = 23.6%) at 2.8 Å resolution. The overall fold is an all β-sheet hybrid. It consists of two sets of four-stranded β-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.

本文言語English
ページ(範囲)2806-2810
ページ数5
ジャーナルProtein Science
13
10
DOI
出版ステータスPublished - 2004 10月
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学

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