4OXI

Crystal structure of Vibrio cholerae adenylation domain AlmE in complex with glycyl-adenosine-5'-phosphate

4OXI の概要

• エントリーDOI: 10.2210/pdb4oxi/pdb
• 分子名称: Enterobactin synthetase component F-related protein, GLYCYL-ADENOSINE-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: adenylation domain, glycine, atp, glycyl-adenosine-5'-phosphate, ligase
• 由来する生物種: Vibrio cholerae serotype O1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65771.03

構造登録者

Fage, C.D.,Henderson, J.C.,Keatinge-Clay, A.T.,Trent, M.S. (登録日: 2014-02-05, 公開日: 2014-12-31, 最終更新日: 2023-09-27)

主引用文献

Henderson, J.C.,Fage, C.D.,Cannon, J.R.,Brodbelt, J.S.,Keatinge-Clay, A.T.,Trent, M.S.
Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases.
Acs Chem.Biol., 9:2382-2392, 2014

PubMed Abstract: The current pandemic El Tor biotype of O1 Vibrio cholerae is resistant to polymyxins, whereas the previous pandemic strain of the classical biotype is polymyxin sensitive. The almEFG operon found in El Tor V. cholerae confers >100-fold resistance to polymyxins through the glycylation of lipopolysaccharide. Here, we present the mechanistic determination of initial steps in the AlmEFG pathway. We verify that AlmF is an aminoacyl carrier protein and identify AlmE as the enzyme required to activate AlmF as a functional carrier protein. A combination of structural information and activity assays was used to identify a pair of active site residues that are important for mediating AlmE glycine specificity. Overall, the structure of AlmE in complex with its glycyl-adenylate intermediate reveals that AlmE is related to Gram-positive d-alanine/d-alanyl carrier protein ligase, while the trio of proteins in the AlmEFG system forms a chemical pathway that resembles the division of labor in nonribosomal peptide synthetases.

PubMed: 25068415
DOI: 10.1021/cb500438x

実験手法

X-RAY DIFFRACTION (2.261 Å)