1RCH

SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI, 8 STRUCTURES

1RCH の概要

• エントリーDOI: 10.2210/pdb1rch/pdb
• 分子名称: RIBONUCLEASE HI (1 entity in total)
• 機能のキーワード: hydrolase, nuclease, endonuclease, magnesium
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Potential): P0A7Y4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17623.00

構造登録者

Yamazaki, T.,Fujiwara, M.,Kato, T.,Yamasaki, K.,Nagayama, K. (登録日: 1995-06-23, 公開日: 1997-02-12, 最終更新日: 2024-05-22)

主引用文献

Fujiwara, M.,Kato, T.,Yamazaki, T.,Yamasaki, K.,Nagayama, K.
Solution Structure of Ribonuclease Hi from Escherichia Coli
Biol.Pharm.Bull., 23:1147-, 2000

PubMed Abstract: The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1,424 distance constraints between individually assigned polypeptide chain hydrogen atoms. Supplemental geometric constraints of 90phi angles and 12chi1 angles, and the distance constraints of 66 hydrogen bonds were experimentally derived. Using the DADAS90 program that calculates structures in dihedral angle space, 15 structures satisfying almost all constraints were obtained. The average root mean square deviation (RMSD) from the mean structure was 0.75 A for backbone atoms. The RMSD for backbone atoms between the representative NMR structure with the smallest constraint violation and crystal structures was within 1.2 A. Although the NMR and crystal structures thus resemble one another, a significant discrepancy was observed in a region termed 'basic protrusion.' The discrepancy observed in NMR experiments is explained by fluctuation in this region.

PubMed: 11041241

実験手法

SOLUTION NMR