5nsf | pdb_00005nsf
Structure of AzuAla
Structural highlights
Function[SYY_METJA] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[1] Publication Abstract from PubMedAllosteric 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, i.e. localized heating, is required for their investigation. Here, we solve this problem by the site-specific incorporation of the non-canonical amino acid beta (1 azulenyl) L alanine (AzAla) via genetic code expansion. Being an exception to Kasha s rule, AzAla undergoes ultrafast internal conversion and heating after S1 excitation. We endowed PDZ3, a protein interaction domain of postsynaptic density protein 95, with this ultrafast heater at two distinct positions. Using ultrafast IR spectroscopy, we could indeed observe VET from the incorporation sites in the protein to a bound peptide ligand on a picosecond timescale. This approach based on genetically encoded AzAla paves the way for detailed studies of VET and its role for function in a wide range of proteins. Observation of Site-Resolved Vibrational Energy Transfer Using a Genetically Encoded Ultrafast Heater.,Baumann T, Hauf M, Schildhauer F, Eberl KB, Durkin PM, Deniz E, Loffler JG, Acevedo-Rocha CG, Jaric J, Martins BM, Dobbek H, Bredenbeck J, Budisa N Angew Chem Int Ed Engl. 2018 Dec 27. doi: 10.1002/anie.201812995. PMID:30589180[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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