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4R1J

Crystal structure of Arc1p-C

Summary for 4R1J
Entry DOI10.2210/pdb4r1j/pdb
DescriptorGU4 nucleic-binding protein 1, GLYCEROL (3 entities in total)
Functional Keywordsemap, trna binding, trna, rna binding protein
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Cellular locationCytoplasm : P46672
Total number of polymer chains1
Total formula weight22147.27
Authors
Altegoer, F.,Bange, G. (deposition date: 2014-08-06, release date: 2015-02-18, Last modification date: 2023-09-20)
Primary citationGiessen, 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: 25583137
DOI: 10.1002/anie.201410047
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

238582

数据于2025-07-09公开中

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