1T0K

Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex

「1CK5」から置き換えられました 「1CK8」から置き換えられました 「1CN8」から置き換えられました 「1CN9」から置き換えられました

1T0K の概要

• エントリーDOI: 10.2210/pdb1t0k/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900010
• 分子名称: 5'-R(*GP*AP*CP*CP*GP*GP*AP*GP*UP*GP*UP*CP*C)-3', 5'-R(*G*GP*AP*CP*GP*CP*AP*GP*AP*GP*AP*UP*GP*GP*UP*C)-3', Maltose-binding periplasmic protein, ... (5 entities in total)
• 機能のキーワード: joint nmr and x-ray refinement, ribosomal protein l30e, mbp fusion protein, ribosome
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Periplasm: P02928; Cytoplasm (By similarity): P14120
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63255.85

構造登録者

Chao, J.A.,Williamson, J.R. (登録日: 2004-04-09, 公開日: 2004-07-20, 最終更新日: 2024-05-22)

主引用文献

Chao, J.A.,Williamson, J.R.
Joint X-Ray and NMR Refinement of the Yeast L30e-mRNA Complex
Structure, 12:1165-1176, 2004

PubMed Abstract: L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own expression by binding to a purine-rich asymmetric internal loop located in both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e fusion protein in complex with an RNA containing the pre-mRNA regulatory site was solved at 3.24 A. Interestingly, the structure of the RNA differed from that observed in a previously determined NMR structure of the complex. Analysis of the NMR data led to the identification of a single imino proton resonance in the internal loop that had been incorrectly assigned and was principally responsible for the erroneous RNA structure. A structure refinement was performed using both the X-ray diffraction data and the NMR-derived distance and angle restraints. The joint NMR and X-ray refinement resulted in improved stereochemistry and lower crystallographic R factors. The RNA internal loop of the MBP-L30e-mRNA complex adopts the canonical K-turn fold.

PubMed: 15242593
DOI: 10.1016/j.str.2004.04.023

実験手法

X-RAY DIFFRACTION (3.24 Å)