7ULA

Structure of the Pseudomonas putida AlgKX modification and secretion complex

7ULA の概要

• エントリーDOI: 10.2210/pdb7ula/pdb
• 分子名称: Alginate biosynthesis protein AlgK, Alginate biosynthesis protein AlgX, NICKEL (II) ION, ... (6 entities in total)
• 機能のキーワード: acetyltransferase, tpr, complex, sugar binding protein, transferase
• 由来する生物種: Pseudomonas putida; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105661.21

構造登録者

Gheorghita, A.A.,Li, E.Y.,Pfoh, R.,Howell, P.L. (登録日: 2022-04-04, 公開日: 2022-12-14, 最終更新日: 2024-10-23)

主引用文献

Gheorghita, A.A.,Li, Y.E.,Kitova, E.N.,Bui, D.T.,Pfoh, R.,Low, K.E.,Whitfield, G.B.,Walvoort, M.T.C.,Zhang, Q.,Codee, J.D.C.,Klassen, J.S.,Howell, P.L.
Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa.
Nat Commun, 13:7631-7631, 2022

PubMed Abstract: Synthase-dependent secretion systems are a conserved mechanism for producing exopolysaccharides in Gram-negative bacteria. Although widely studied, it is not well understood how these systems are organized to coordinate polymer biosynthesis, modification, and export across both membranes and the peptidoglycan. To investigate how synthase-dependent secretion systems produce polymer at a molecular level, we determined the crystal structure of the AlgK-AlgX (AlgKX) complex involved in Pseudomonas aeruginosa alginate exopolysaccharide acetylation and export. We demonstrate that AlgKX directly binds alginate oligosaccharides and that formation of the complex is vital for polymer production and biofilm attachment. Finally, we propose a structural model for the AlgEKX outer membrane modification and secretion complex. Together, our study provides insight into how alginate biosynthesis proteins coordinate production of a key exopolysaccharide involved in establishing persistent Pseudomonas lung infections.

PubMed: 36494359
DOI: 10.1038/s41467-022-35131-6

実験手法

X-RAY DIFFRACTION (2.46 Å)