3A1R

Neutron crystal structure analysis of bovine pancreatic ribonuclease A

3A1R の概要

• エントリーDOI: 10.2210/pdb3a1r/pdb
• 分子名称: Ribonuclease pancreatic (2 entities in total)
• 機能のキーワード: bovine pancreatic ribonuclease a, neutron structure, endonuclease, glycation, glycoprotein, hydrolase, secreted, disulfide bond, nuclease
• 由来する生物種: Bos taurus (Bovine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13708.33

構造登録者

Yagi, D.,Tanaka, I.,Niimura, N. (登録日: 2009-04-21, 公開日: 2009-09-01, 最終更新日: 2024-11-06)

主引用文献

Yagi, D.,Yamada, T.,Kurihara, K.,Ohnishi, Y.,Yamashita, M.,Tamada, T.,Tanaka, I.,Kuroki, R.,Niimura, N.
A neutron crystallographic analysis of phosphate-free ribonuclease A at 1.7 A resolution
Acta Crystallogr.,Sect.D, 65:892-899, 2009

PubMed Abstract: A neutron crystallographic analysis of phosphate-free bovine pancreatic RNase A has been carried out at 1.7 A resolution using the BIX-4 single-crystal diffractometer at the JRR-3 reactor of the Japan Atomic Energy Agency. The high-resolution structural model allowed us to determine that His12 acts mainly as a general base in the catalytic process of RNase A. Numerous other distinctive structural features such as the hydrogen positions of methyl groups, hydroxyl groups, prolines, asparagines and glutamines were also determined at 1.7 A resolution. The protonation and deprotonation states of all of the charged amino-acid residues allowed us to provide a definitive description of the hydrogen-bonding network around the active site and the H atoms of the key His48 residue. Differences in hydrogen-bond strengths for the alpha-helices and beta-sheets were inferred from determination of the hydrogen-bond lengths and the H/D-exchange ratios of the backbone amide H atoms. The correlation between the B factors and hydrogen-bond lengths of the hydration water molecules was also determined.

PubMed: 19690366
DOI: 10.1107/S0907444909018885

実験手法

NEUTRON DIFFRACTION