2KHJ

NMR structure of the domain 6 of the E. coli ribosomal protein S1

2KHJ の概要

• エントリーDOI: 10.2210/pdb2khj/pdb
• 分子名称: 30S ribosomal protein S1 (1 entity in total)
• 機能のキーワード: ribosomal protein s1, ob fold, acetylation, phosphoprotein, ribonucleoprotein, ribosomal protein, rna-binding
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11710.04

構造登録者

Salah, P.,Bisaglia, M.,Aliprandi, P.,Uzan, M.,Sizun, C.,Bontems, F. (登録日: 2009-04-07, 公開日: 2009-10-20, 最終更新日: 2024-05-29)

主引用文献

Salah, P.,Bisaglia, M.,Aliprandi, P.,Uzan, M.,Sizun, C.,Bontems, F.
Probing the relationship between Gram-negative and Gram-positive S1 proteins by sequence analysis
Nucleic Acids Res., 37:5578-5588, 2009

PubMed Abstract: Escherichia coli ribosomal protein S1 is required for the translation initiation of messenger RNAs, in particular when their Shine-Dalgarno sequence is degenerated. Closely related forms of the protein, composed of the same number of domains (six), are found in all Gram-negative bacteria. More distant proteins, generally formed of fewer domains, have been identified, by sequence similarities, in Gram-positive bacteria and are also termed 'S1 proteins'. However in the absence of functional information, it is generally difficult to ascertain their relationship with Gram-negative S1. In this article, we report the solution structure of the fourth and sixth domains of the E. coli protein S1 and show that it is possible to characterize their beta-barrel by a consensus sequence that allows a precise identification of all domains in Gram-negative and Gram-positive S1 proteins. In addition, we show that it is possible to discriminate between five domain types corresponding to the domains 1, 2, 3, 4-5 and 6 of E. coli S1 on the basis of their sequence. This enabled us to identify the nature of the domains present in Gram-positive proteins and, subsequently, to probe the filiations between all forms of S1.

PubMed: 19605565
DOI: 10.1093/nar/gkp547

実験手法

SOLUTION NMR