5NSF

Structure of AzuAla

Summary for 5NSF

• Entry DOI: 10.2210/pdb5nsf/pdb
• Descriptor: Tyrosine--tRNA ligase, (2~{S})-2-azanyl-3-(2,6-dihydroazulen-1-yl)propanoic acid, GLYCEROL, ... (6 entities in total)
• Functional Keywords: nnca, ligase
• Biological source: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
• Total number of polymer chains: 4
• Total formula weight: 146848.36

Authors

Martins, B.M. (deposition date: 2017-04-26, release date: 2019-01-16, Last modification date: 2024-01-17)

Primary citation

Baumann, T.,Hauf, M.,Schildhauer, F.,Eberl, K.B.,Durkin, P.M.,Deniz, E.,Loffler, J.G.,Acevedo-Rocha, C.G.,Jaric, J.,Martins, B.M.,Dobbek, H.,Bredenbeck, J.,Budisa, N.
Site-Resolved Observation of Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater.
Angew. Chem. Int. Ed. Engl., 58:2899-2903, 2019

PubMed Abstract: Allosteric information transfer in proteins has been linked to distinct vibrational energy transfer (VET) pathways in a number of theoretical studies. Experimental evidence for such pathways, however, is sparse because site-selective injection of vibrational energy into a protein, that is, localized heating, is required for their investigation. Here, we solved this problem by the site-specific incorporation of the non-canonical amino acid β-(1-azulenyl)-l-alanine (AzAla) through genetic code expansion. As an exception to Kasha's rule, AzAla undergoes ultrafast internal conversion and heating after S excitation while upon S excitation, it serves as a fluorescent label. We equipped PDZ3, a protein interaction domain of postsynaptic density protein 95, with this ultrafast heater at two distinct positions. We indeed observed VET from the incorporation sites in the protein to a bound peptide ligand on the picosecond timescale by ultrafast IR spectroscopy. This approach based on genetically encoded AzAla paves the way for detailed studies of VET and its role in a wide range of proteins.

PubMed: 30589180
DOI: 10.1002/anie.201812995

Experimental method

X-RAY DIFFRACTION (2.426 Å)