1CK2

YEAST (SACCHAROMYCES CEREVISIAE) RIBOSOMAL PROTEIN L30

1CK2 の概要

• エントリーDOI: 10.2210/pdb1ck2/pdb
• 分子名称: 60S RIBOSOMAL PROTEIN L30 (1 entity in total)
• 機能のキーワード: ribosomal protein, auto-regulation of pre-mrna splicing and mrna translation, ribosome
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11299.17

構造登録者

Mao, H.,Willamson, J.R. (登録日: 1999-04-26, 公開日: 1999-10-14, 最終更新日: 2023-12-27)

主引用文献

Mao, H.,Williamson, J.R.
Local folding coupled to RNA binding in the yeast ribosomal protein L30
J.Mol.Biol., 292:345-359, 1999

PubMed Abstract: The ribosomal protein L30 from yeast Saccharomyces cerevisiae auto-regulates its own synthesis by binding to a structural element in both its pre-mRNA and its mRNA. The three-dimensional structures of L30 in the free (f L30) and the pre-mRNA bound (b L30) forms have been solved by nuclear magnetic resonance spectroscopy. Both protein structures contain four alternating alpha-helices and four beta-strands segments and adopt an overall topology that is an alphabetaalpha three-layer sandwich, representing a unique fold. Three loops on one end of the alphabetaalpha sandwich have been mapped as the RNA binding site on the basis of structural comparison, chemical shift perturbation and the inter-molecular nuclear Overhauser effects to the RNA. The structural and dynamic comparison of f L30 and b L30 reveals that local dynamics may play an important role in the RNA binding. The fourth helix in b L30 is longer than in f L30, and is stabilized by RNA binding. The exposed hydrophobic surface that is buried upon RNA binding may provide the energy necessary to drive secondary structure formation, and may account for the increased stability of b L30.

PubMed: 10493880
DOI: 10.1006/jmbi.1999.3044

実験手法

SOLUTION NMR