8A1C

TraI trans-esterase domain from pKM101 (DNA bound)

8A1C の概要

• エントリーDOI: 10.2210/pdb8a1c/pdb
• 関連するPDBエントリー: 8A1B
• 分子名称: TraI, 11mer oriT DNA, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: relaxase, dna binding protein, trans-esterase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38227.97

構造登録者

Breidenstein, A.,Berntsson, R.P.-A. (登録日: 2022-06-01, 公開日: 2022-07-13, 最終更新日: 2024-02-07)

主引用文献

Breidenstein, A.,Ter Beek, J.,Berntsson, R.P.
Structural and functional characterization of TraI from pKM101 reveals basis for DNA processing.
Life Sci Alliance, 6:-, 2023

PubMed Abstract: Type 4 secretion systems are large and versatile protein machineries that facilitate the spread of antibiotic resistance and other virulence factors via horizontal gene transfer. Conjugative type 4 secretion systems depend on relaxases to process the DNA in preparation for transport. TraI from the well-studied conjugative plasmid pKM101 is one such relaxase. Here, we report the crystal structure of the trans-esterase domain of TraI in complex with its substrate DNA, highlighting the conserved DNA-binding mechanism of conjugative relaxases. In addition, we present an apo structure of the trans-esterase domain of TraI that includes most of the flexible thumb region. This allows us for the first time to visualize the large conformational change of the thumb subdomain upon DNA binding. We also characterize the DNA binding, nicking, and religation activity of the trans-esterase domain, helicase domain, and full-length TraI. Unlike previous indications in the literature, our results reveal that the TraI trans-esterase domain from pKM101 behaves in a conserved manner with its homologs from the R388 and F plasmids.

PubMed: 36669792
DOI: 10.26508/lsa.202201775

実験手法

X-RAY DIFFRACTION (2.1 Å)