5L7P

In silico-powered specific incorporation of photocaged Dopa at multiple protein sites

Summary for 5L7P

• Entry DOI: 10.2210/pdb5l7p/pdb
• Descriptor: Tyrosine--tRNA ligase, PENTAETHYLENE GLYCOL, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: tyrrs, ligase
• Biological source: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
• Cellular location: Cytoplasm: Q57834
• Total number of polymer chains: 2
• Total formula weight: 73378.63

Authors

Hauf, M.,Richter, F.,Schneider, T.,Martins, B.M.,Baumann, T.,Durkin, P.,Dobbek, H.,Moeglich, A.,Budisa, N. (deposition date: 2016-06-03, release date: 2017-09-13, Last modification date: 2024-01-10)

Primary citation

Hauf, M.,Richter, F.,Schneider, T.,Faidt, T.,Martins, B.M.,Baumann, T.,Durkin, P.,Dobbek, H.,Jacobs, K.,Moglich, A.,Budisa, N.
Photoactivatable Mussel-Based Underwater Adhesive Proteins by an Expanded Genetic Code.
Chembiochem, 18:1819-1823, 2017

PubMed Abstract: Marine mussels exhibit potent underwater adhesion abilities under hostile conditions by employing 3,4-dihydroxyphenylalanine (DOPA)-rich mussel adhesive proteins (MAPs). However, their recombinant production is a major biotechnological challenge. Herein, a novel strategy based on genetic code expansion has been developed by engineering efficient aminoacyl-transfer RNA synthetases (aaRSs) for the photocaged noncanonical amino acid ortho-nitrobenzyl DOPA (ONB-DOPA). The engineered ONB-DOPARS enables in vivo production of MAP type 5 site-specifically equipped with multiple instances of ONB-DOPA to yield photocaged, spatiotemporally controlled underwater adhesives. Upon exposure to UV light, these proteins feature elevated wet adhesion properties. This concept offers new perspectives for the production of recombinant bioadhesives.

PubMed: 28650092
DOI: 10.1002/cbic.201700327

Experimental method

X-RAY DIFFRACTION (1.9 Å)