1N88

NMR structure of the ribosomal protein L23 from Thermus thermophilus.

1N88 の概要

• エントリーDOI: 10.2210/pdb1n88/pdb
• 分子名称: Ribosomal protein L23 (1 entity in total)
• 機能のキーワード: nmr spectroscopy, protein structure, l23, ribosome, translation
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10759.81

構造登録者

Ohman, A.,Rak, A.,Dontsova, M.,Garber, M.B.,Hard, T. (登録日: 2002-11-20, 公開日: 2003-06-10, 最終更新日: 2024-05-29)

主引用文献

Ohman, A.,Rak, A.,Dontsova, M.,Garber, M.B.,Hard, T.
NMR structure of the ribosomal protein L23 from Thermus thermophilus.
J.Biomol.NMR, 26:131-137, 2003

PubMed Abstract: The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed.

PubMed: 12766408
DOI: 10.1023/A:1023502307069

実験手法

SOLUTION NMR