7CPH

Crystal structure of tRNA adenosine deaminase from Bacillus subtilis

7CPH の概要

• エントリーDOI: 10.2210/pdb7cph/pdb
• 分子名称: tRNA-specific adenosine deaminase, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: hydrolase, trna adenosine deaminase
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37259.76

構造登録者

Gaded, V.,Mariam, J.,Anand, R. (登録日: 2020-08-07, 公開日: 2021-06-02, 最終更新日: 2023-11-29)

主引用文献

Mariam, J.,Hoskere Ashoka, A.,Gaded, V.,Ali, F.,Malvi, H.,Das, A.,Anand, R.
Deciphering protein microenvironment by using a cysteine specific switch-ON fluorescent probe.
Org.Biomol.Chem., 19:5161-5168, 2021

PubMed Abstract: Fluorescent probes provide an unparalleled opportunity to visualize and quantify dynamic events. Here, we employ a medium-size, cysteine specific coumarin based switch-ON fluorescent probe 'L' to track protein unfolding profiles and accessibility of cysteine residues in proteins. It was established that 'L' is highly selective and exhibits no artifact due to interaction with other bystander species. 'L' is able to gauge subtle changes in protein microenvironment and proved to be effective in delineating early unfolding events that are difficult to otherwise discern by classic techniques such as circular dichroism. By solving the X-ray structure of TadA and probing the temperature dependent fluorescence-ON response with native TadA and its cysteine mutants, it was revealed that unfolding occurs in a stage-wise manner and the regions that are functionally important form compact sub-domains and unfold at later stages. Our results assert that probe 'L' serves as an efficient tool to monitor subtle changes in protein structure and can be employed as a generic dye to study processes such as protein unfolding.

PubMed: 34037063
DOI: 10.1039/d1ob00698c

実験手法

X-RAY DIFFRACTION (2.3 Å)