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9EXP

Wzc-K540M-2YE MgADP C8

9EXP の概要
エントリーDOI10.2210/pdb9exp/pdb
EMDBエントリー50043
分子名称Putative transmembrane protein Wzc, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
機能のキーワードwzc-k540m-2ye, membrane protein
由来する生物種Escherichia coli
タンパク質・核酸の鎖数8
化学式量合計647637.80
構造登録者
Liu, J.W.,Yang, Y.,Naismith, J.H. (登録日: 2024-04-08, 公開日: 2025-04-23, 最終更新日: 2025-07-02)
主引用文献Yang, Y.,Batista, M.,Clarke, B.R.,Agyare-Tabbi, M.R.,Song, H.,Kuehfuss, N.M.,Le Bas, A.,Robinson, C.V.,Whitfield, C.,Stansfeld, P.J.,Naismith, J.H.,Liu, J.
Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc.
Nat Commun, 16:3437-3437, 2025
Cited by
PubMed Abstract: The regulation of polymerisation and translocation of biomolecules is fundamental. Wzc, an integral cytoplasmic membrane tyrosine autokinase protein serves as the master regulator of the biosynthesis and export of many bacterial capsular polysaccharides and exopolysaccharides. Such polysaccharides play essential roles in infection, defence, and some are important industrial products. Wzc comprises a large periplasmic domain, two transmembrane helices and a C-terminal cytoplasmic kinase domain with a tyrosine-rich tail. Wzc regulates polymerisation functions through cycling the formation and dissociation of an octameric complex, driven by changes in the phosphorylation status of the tyrosine-rich tail. E. coli Wzc serves a model for a wider family of polysaccharide co-polymerases. Here, we determine structures of intermediate states with different extents of phosphorylation. Structural and computational data reveal the pre-ordering of the tyrosine-rich tail, the molecular basis underlying the unidirectionality of phosphorylation events, and the underlying structural dynamics on how phosphorylation status is transmitted.
PubMed: 40210632
DOI: 10.1038/s41467-025-58693-7
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.85 Å)
構造検証レポート
Validation report summary of 9exp
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2026-04-01に公開中

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