4R1J
Crystal structure of Arc1p-C
Summary for 4R1J
Entry DOI | 10.2210/pdb4r1j/pdb |
Descriptor | GU4 nucleic-binding protein 1, GLYCEROL (3 entities in total) |
Functional Keywords | emap, trna binding, trna, rna binding protein |
Biological source | Saccharomyces cerevisiae (Baker's yeast) |
Cellular location | Cytoplasm : P46672 |
Total number of polymer chains | 1 |
Total formula weight | 22147.27 |
Authors | Altegoer, F.,Bange, G. (deposition date: 2014-08-06, release date: 2015-02-18, Last modification date: 2023-09-20) |
Primary citation | Giessen, T.W.,Altegoer, F.,Nebel, A.J.,Steinbach, R.M.,Bange, G.,Marahiel, M.A. A Synthetic Adenylation-Domain-Based tRNA-Aminoacylation Catalyst. Angew.Chem.Int.Ed.Engl., 54:2492-2496, 2015 Cited by PubMed Abstract: The incorporation of non-proteinogenic amino acids represents a major challenge for the creation of functionalized proteins. The ribosomal pathway is limited to the 20-22 proteinogenic amino acids while nonribosomal peptide synthetases (NRPSs) are able to select from hundreds of different monomers. Introduced herein is a fusion-protein-based design for synthetic tRNA-aminoacylation catalysts based on combining NRPS adenylation domains and a small eukaryotic tRNA-binding domain (Arc1p-C). Using rational design, guided by structural insights and molecular modeling, the adenylation domain PheA was fused with Arc1p-C using flexible linkers and achieved tRNA-aminoacylation with both proteinogenic and non-proteinogenic amino acids. The resulting aminoacyl-tRNAs were functionally validated and the catalysts showed broad substrate specificity towards the acceptor tRNA. Our strategy shows how functional tRNA-aminoacylation catalysts can be created for bridging the ribosomal and nonribosomal worlds. This opens up new avenues for the aminoacylation of tRNAs with functional non-proteinogenic amino acids. PubMed: 25583137DOI: 10.1002/anie.201410047 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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