RpbL12 Assists Catalysis by Correctly Positioning the Incoming Aminoacyl-tRNA in the A-Site of E. coli 70S Ribosomes.

Jean-Bernard Créchet,Fulbert K Agbo'Saga,Soria Baouz,Codjo Hountondj

The open biochemistry journal（2018）

Cited 3|Views6

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Abstract

This α-NH group is likely to be generated by the unprotonated εNH form of Lys-65 which is capable of withdrawing a proton from the α-NH group of aa-tRNA.

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Key words

Aminoacyl-tRNA,E. coli ribosomal protein bL12,GGQ-like GAN motif of bL12,Lys-65 of bL12,Mechanism of peptide bond formation,Site-directed mutagenesis

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