1AD2

RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE

1AD2 の概要

• エントリーDOI: 10.2210/pdb1ad2/pdb
• 分子名称: RIBOSOMAL PROTEIN L1, SULFATE ION, MERCURY (II) ION, ... (5 entities in total)
• 機能のキーワード: ribosomal protein, rna binding, protein synthesis, mutant
• 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: 25359.52

構造登録者

Unge, J.,Al-Karadaghi, S.,Liljas, A.,Jonsson, B.-H.,Eliseikina, I.,Ossina, N.,Nevskaya, N.,Fomenkova, N.,Garber, M.,Nikonov, S. (登録日: 1997-02-20, 公開日: 1997-05-15, 最終更新日: 2024-02-07)

主引用文献

Unge, J.,Al-Karadaghi, S.,Liljas, A.,Jonsson, B.H.,Eliseikina, I.,Ossina, N.,Nevskaya, N.,Fomenkova, N.,Garber, M.,Nikonov, S.
A mutant form of the ribosomal protein L1 reveals conformational flexibility.
FEBS Lett., 411:53-59, 1997

PubMed Abstract: The crystal structure of the mutant S179C of the ribosomal protein L1 from Thermus thermophilus has been determined at 1.9 A resolution. The mutant molecule displays a small but significant opening of the cavity between the two domains. The domain movement seems to be facilitated by the flexibility of at least two conserved glycines. These glycines may be necessary for the larger conformational change needed for an induced fit mechanism upon binding RNA. The domain movement makes a disulfide bridge possible between the incorporated cysteines in two monomers of the mutant L1.

PubMed: 9247141
DOI: 10.1016/S0014-5793(97)00611-X

実験手法

X-RAY DIFFRACTION (1.9 Å)