1V9H

Crystal structure of the RNase MC1 mutant Y101A in complex with 5'-UMP

1V9H の概要

• エントリーDOI: 10.2210/pdb1v9h/pdb
• 分子名称: Ribonuclease MC, SULFATE ION, URIDINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: hydolase, nucleic acid, rna, hydrolase
• 由来する生物種: Momordica charantia (balsam pear)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22540.07

構造登録者

Kimura, K.,Numata, T.,Kakuta, Y.,Kimura, M. (登録日: 2004-01-26, 公開日: 2004-10-05, 最終更新日: 2024-10-16)

主引用文献

Kimura, K.,Numata, T.,Kakuta, Y.,Kimura, M.
Amino acids conserved at the C-terminal half of the ribonuclease t2 family contribute to protein stability of the enzymes
Biosci.Biotechnol.Biochem., 68:1748-1757, 2004

PubMed Abstract: The ribonuclease MC1 (RNase MC1) from the seeds of the bitter gourd belongs to the RNase T2 family. We evaluated the contribution of 11 amino acids conserved in the RNase T2 family to protein folding of RNase MC1. Thermal unfolding experiments showed that substitution of Tyr(101), Phe(102), Ala(105), and Phe(190) resulted in a significant decrease in themostability; the T(m) values were 47-58 degrees C compared to that for the wild type (64 degrees C). Mutations of Pro(125), Gly(127), Gly(144), and Val(165) caused a moderate decrease in thermostability (T(m): 60-62 degrees C). In contrast, mutations of Asp(107) and Gly(173) did little effect on thermostability. The contribution of Tyr(101), Phe(102), Pro(125), and Gly(127) to protein stability was further corroborated by means of Gdn-HCl unfolding and protease digestions. Taken together, it appeared that Tyr(101), Phe(102), Ala(105), Pro(125), Gly(127), Gly(144), Leu(162), Val(165), and Phe(190) conserved in the RNase T2 family play an important role in the stability of the proteins.

PubMed: 15322360
DOI: 10.1271/bbb.68.1748

実験手法

X-RAY DIFFRACTION (2 Å)