1V8Q

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8

1V8Q の概要

• エントリーDOI: 10.2210/pdb1v8q/pdb
• 分子名称: TT0826, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• 機能のキーワード: structural genomics, proteomics, riken structural genomics/proteomics initiative, rsgi, translation
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 38270.55

構造登録者

Wang, H.,Takemoto-Hori, C.,Murayama, K.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-01-13, 公開日: 2004-07-13, 最終更新日: 2023-12-27)

主引用文献

Wang, H.,Takemoto-Hori, C.,Murayama, K.,Sakai, H.,Tatsuguchi, A.,Terada, T.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.
Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8
Protein Sci., 13:2806-2810, 2004

PubMed 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 A 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.

PubMed: 15340170
DOI: 10.1110/ps.04864904

実験手法

X-RAY DIFFRACTION (2.8 Å)