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6A82

Crystal structure of the C-terminal periplasmic domain of EcEptC from Escherichia coli

6A82 の概要
エントリーDOI10.2210/pdb6a82/pdb
分子名称Phosphoethanolamine transferase EptC, SODIUM ION (3 entities in total)
機能のキーワードphosphoethanolamine transferase, transferase
由来する生物種Escherichia coli
タンパク質・核酸の鎖数3
化学式量合計138085.35
構造登録者
Zhao, Y.Q.,Gu, Y.J.,Cheng, W. (登録日: 2018-07-06, 公開日: 2018-12-26, 最終更新日: 2024-11-06)
主引用文献Zhao, Y.,Meng, Q.,Lai, Y.,Wang, L.,Zhou, D.,Dou, C.,Gu, Y.,Nie, C.,Wei, Y.,Cheng, W.
Structural and mechanistic insights into polymyxin resistance mediated by EptC originating from Escherichia coli.
FEBS J., 286:750-764, 2019
Cited by
PubMed Abstract: Gram-negative bacteria defend against the toxicity of polymyxins by modifying their outer membrane lipopolysaccharide (LPS). This modification mainly occurs through the addition of cationic molecules such as phosphoethanolamine (PEA). EcEptC is a PEA transferase from Escherichia coli (E. coli). However, unlike its homologs CjEptC (Campylobacter jejuni) and MCR-1, EcEptC is unable to mediate polymyxin resistance when overexpressed in E. coli. Here, we report crystal structures of the C-terminal putative catalytic domain (EcEptCΔN, 205-577 aa) of EcEptC in apo and Zn -bound states at 2.10 and 2.60 Å, respectively. EcEptCΔN is arranged into an α-β-α fold and equipped with the zinc ion in a conserved mode. Coupled with isothermal titration calorimetry (ITC) data, we provide insights into the mechanism by which EcEptC recognizes Zn . Furthermore, structure comparison analysis indicated that disulfide bonds, which play a key role in polymyxin resistance, were absent in EcEptCΔN. Supported by structural and biochemical evidence, we reveal mechanistic implications for disulfide bonds in PEA transferase-mediated polymyxin resistance. Significantly, because the structural effects exhibited by disulfide bonds are absent in EcEptC, it is impossible for this protein to participate in polymyxin resistance in E. coli. DATABASE: Structural data are available in the PDB under the accession numbers 6A82 and 6A83. ENZYME: EC 2.7.8.43.
PubMed: 30537137
DOI: 10.1111/febs.14719
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 6a82
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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