6Y3G

Crystal structure of phenylalanine tRNA from Escherichia coli

6Y3G の概要

• エントリーDOI: 10.2210/pdb6y3g/pdb
• 分子名称: RNA (75-MER), GUANIDINE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: transfer rna with modifications, rna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25229.69

構造登録者

Bourgeois, G.,Mechulam, Y.,Schmitt, E. (登録日: 2020-02-18, 公開日: 2020-12-30, 最終更新日: 2024-01-24)

主引用文献

Bourgeois, G.,Seguin, J.,Babin, M.,Gondry, M.,Mechulam, Y.,Schmitt, E.
Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates.
Rna, 26:1589-1602, 2020

PubMed Abstract: Cyclodipeptide synthases (CDPSs) catalyze the synthesis of various cyclodipeptides by using two aminoacyl-tRNA (aa-tRNA) substrates in a sequential mechanism. Here, we studied binding of phenylalanyl-tRNA to the CDPS from (-CDPS) by gel filtration and electrophoretic mobility shift assay. We determined the crystal structure of the -CDPS:Phe-tRNA complex to 5 Å resolution and further studied it in solution using small-angle X-ray scattering (SAXS). The data show that the major groove of the acceptor stem of the aa-tRNA interacts with the enzyme through the basic β2 and β7 strands of CDPSs belonging to the XYP subfamily. A bending of the CCA extremity enables the amino acid moiety to be positioned in the P1 pocket while the terminal A76 adenosine occupies the P2 pocket. Such a positioning indicates that the present structure illustrates the binding of the first aa-tRNA. In cells, CDPSs and the elongation factor EF-Tu share aminoacylated tRNAs as substrates. The present study shows that CDPSs and EF-Tu interact with opposite sides of tRNA. This may explain how CDPSs hijack aa-tRNAs from canonical ribosomal protein synthesis.

PubMed: 32680846
DOI: 10.1261/rna.075184.120

実験手法

X-RAY DIFFRACTION (3.1 Å)