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

doi:10.1110/ps.04864904

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

MEN - Biomedical Engineering

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	2806-2810
Number of pages	5
Journal	Protein Science
Volume	13
Issue number	10
DOIs	https://doi.org/10.1110/ps.04864904
Publication status	Published - 2004 Oct

Keywords

Crystal structure
Protein-RNA interactions
Ribosomal protein L27
Ribosome
Thermus thermophilus HB8

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title = "Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8",

abstract = "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 {\AA} 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.",

keywords = "Crystal structure, Protein-RNA interactions, Ribosomal protein L27, Ribosome, Thermus thermophilus HB8",

author = "Hongfei Wang and Takemoto, {Chie Hori} and Kazutaka Murayama and Hiroaki Sakai and Ayako Tatsuguchi and Takaho Terada and Mikako Shirouzu and Seiki Kuramitsu and Shigeyuki Yokoyama",

year = "2004",

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language = "English",

volume = "13",

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journal = "Protein Science",

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T1 - Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

AU - Wang, Hongfei

AU - Takemoto, Chie Hori

AU - Murayama, Kazutaka

AU - Sakai, Hiroaki

AU - Tatsuguchi, Ayako

AU - Terada, Takaho

AU - Shirouzu, Mikako

AU - Kuramitsu, Seiki

AU - Yokoyama, Shigeyuki

PY - 2004/10

Y1 - 2004/10

N2 - 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.

AB - 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.

KW - Crystal structure

KW - Protein-RNA interactions

KW - Ribosomal protein L27

KW - Ribosome

KW - Thermus thermophilus HB8

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JO - Protein Science

JF - Protein Science

IS - 10

ER -

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

Abstract

Keywords

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