4NX2

Crystal structure of DCYRS complexed with DCY

Summary for 4NX2

• Entry DOI: 10.2210/pdb4nx2/pdb
• Descriptor: Tyrosine--tRNA ligase, 3,5-dichloro-L-tyrosine (3 entities in total)
• Functional Keywords: ligase activity, translation, nucleotide, ligase
• Biological source: Methanocaldococcus jannaschii
• Cellular location: Cytoplasm: Q57834
• Total number of polymer chains: 1
• Total formula weight: 35956.65

Authors

Wang, J.,Gong, W.,Li, J.,Gao, F.,Li, H. (deposition date: 2013-12-08, release date: 2014-09-24, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)