4NX2

Crystal structure of DCYRS complexed with DCY

4NX2 の概要

• エントリーDOI: 10.2210/pdb4nx2/pdb
• 分子名称: Tyrosine--tRNA ligase, 3,5-dichloro-L-tyrosine (3 entities in total)
• 機能のキーワード: ligase activity, translation, nucleotide, ligase
• 由来する生物種: Methanocaldococcus jannaschii
• 細胞内の位置: Cytoplasm: Q57834
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35956.65

構造登録者

Wang, J.,Gong, W.,Li, J.,Gao, F.,Li, H. (登録日: 2013-12-08, 公開日: 2014-09-24, 最終更新日: 2024-05-29)

主引用文献

Liu, X.,Jiang, L.,Li, J.,Wang, L.,Yu, Y.,Zhou, Q.,Lv, X.,Gong, W.,Lu, Y.,Wang, J.
Significant expansion of fluorescent protein sensing ability through the genetic incorporation of superior photo-induced electron-transfer quenchers.
J.Am.Chem.Soc., 136:13094-13097, 2014

PubMed Abstract: Photo-induced electron transfer (PET) is ubiquitous for photosynthesis and fluorescent sensor design. However, genetically coded PET sensors are underdeveloped, due to the lack of methods to site-specifically install PET probes on proteins. Here we describe a family of acid and Mn(III) turn-on fluorescent protein (FP) sensors, named iLovU, based on PET and the genetic incorporation of superior PET quenchers in the fluorescent flavoprotein iLov. Using the iLovU PET sensors, we monitored the cytoplasmic acidification process, and achieved Mn(III) fluorescence sensing for the first time. The iLovU sensors should be applicable for studying pH changes in living cells, monitoring biogentic Mn(III) in the environment, and screening for efficient manganese peroxidase, which is highly desirable for lignin degradation and biomass conversion. Our work establishes a platform for many more protein PET sensors, facilitates the de novo design of metalloenzymes harboring redox active residues, and expands our ability to probe protein conformational dynamics.

PubMed: 25197956
DOI: 10.1021/ja505219r

実験手法

X-RAY DIFFRACTION (2 Å)