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Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8
Author(s) -
Wang Hongfei,
Takemoto Chie Hori,
Murayama Kazutaka,
Sakai Hiroaki,
Tatsuguchi Ayako,
Terada Takaho,
Shirouzu Mikako,
Kuramitsu Seiki,
Yokoyama Shigeyuki
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04864904
Subject(s) - thermus thermophilus , ribosomal protein , ribosomal rna , 5s ribosomal rna , 50s , crystallography , ribosome , crystal structure , eukaryotic large ribosomal subunit , biology , rna , chemistry , biochemistry , 18s ribosomal rna , escherichia coli , gene
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 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.