An orthogonal seryl-tRNA synthetase/tRNA pair for noncanonical amino acid mutagenesis in Escherichia coli!

被引:13
作者
Zambaldo, Claudio [1 ,2 ]
Koh, Minseob [1 ,2 ]
Nasertorabi, Fariborz [3 ,4 ]
Han, Gye Won [3 ,4 ]
Chatterjee, Abhishek [5 ]
Stevens, Raymond C. [3 ,4 ]
Schultz, Peter G. [1 ,2 ]
机构
[1] Scripps Res Inst, Dept Chem, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA
[3] Univ Southern Calif, Michelson Ctr Convergent Biosci, Bridge Inst, Dept Biol Sci, Los Angeles, CA 90089 USA
[4] Univ Southern Calif, Michelson Ctr Convergent Biosci, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA
[5] Boston Coll, Dept Chem, 2609 Beacon St,246B Merkert Chem Ctr, Chestnut Hill, MA 02467 USA
关键词
Seryl-tRNA synthetase; E. coli orthogonality; Genetic code expansion; X-ray crystallography; Non-canonical amino acids; GENETIC-CODE; CRYSTAL-STRUCTURE; THERMUS-THERMOPHILUS; EVOLUTION; AMBER; DISCRIMINATION; PHOSPHOSERINE; MULTIPLE; REVEALS;
D O I
10.1016/j.bmc.2020.115662
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We report the development of the orthogonal amber-suppressor pair Archaeoglobus fulgidus seryl-tRNA (Af-tRNA(Ser))/Methanosarcina mazei seryl-tRNA synthetase (MmSerRS) in Escherichia coli. Furthermore, the crystal structure of MmSerRS was solved at 1.45 angstrom resolution, which should enable structure-guided engineering of its active site to genetically encode small, polar noncanonical amino acids (ncAAs).
引用
收藏
页数:5
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