2BIR

ADDITIVITY OF SUBSTRATE BINDING IN RIBONUCLEASE T1 (Y42A MUTANT)

2BIR の概要

• エントリーDOI: 10.2210/pdb2bir/pdb
• 分子名称: RIBONUCLEASE T1, CALCIUM ION, GUANOSINE-2'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: hydrolase, nuclease, endonuclease, ribonuclease
• 由来する生物種: Aspergillus oryzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11361.89

構造登録者

Doumen, J.,Steyaert, J.,Loverix, S. (登録日: 1996-12-03, 公開日: 1997-06-16, 最終更新日: 2024-10-23)

主引用文献

Loverix, S.,Doumen, J.,Steyaert, J.
Additivity of protein-guanine interactions in ribonuclease T1.
J.Biol.Chem., 272:9635-9639, 1997

PubMed Abstract: It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a structural motif that renders guanine specificity to ribonuclease T1. We report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the guanine specificity of RNase T1. The Y42A and E46A mutations profoundly affect substrate binding. No such effect is observed for Y45A RNase T1. From the kinetics of the Y42A/Y45A and Y42A/E46A double mutants, we conclude that these pairs of residues contribute to guanine specificity in a mutually independent way. From our results, it appears that the energetic contribution of aromatic face-to-face stacking interactions may be significant if polycyclic molecules, such as guanine, are involved.

PubMed: 9092491
DOI: 10.1074/jbc.272.15.9635

実験手法

X-RAY DIFFRACTION (2.3 Å)