5A0F

Crystal structure of Yersinia Afp18-modified RhoA

5A0F の概要

• エントリーDOI: 10.2210/pdb5a0f/pdb
• 分子名称: TRANSFORMING PROTEIN RHOA, GUANOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: signaling protein, n-acetylglucosamine-protein, tyrosine glycosylation, gtpase, bacterial toxin effector, type 6 secretion system, antifeeding prophage
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21227.93

構造登録者

Jank, T.,Schimpl, M.,van Aalten, D.M. (登録日: 2015-04-20, 公開日: 2015-07-22, 最終更新日: 2024-10-23)

主引用文献

Jank, T.,Eckerle, S.,Steinemann, M.,Trillhaase, C.,Schimpl, M.,Wiese, S.,van Aalten, D.M.,Driever, W.,Aktories, K.
Tyrosine glycosylation of Rho by Yersinia toxin impairs blastomere cell behaviour in zebrafish embryos.
Nat Commun, 6:7807-7807, 2015

PubMed Abstract: Yersinia species cause zoonotic infections, including enterocolitis and plague. Here we studied Yersinia ruckeri antifeeding prophage 18 (Afp18), the toxin component of the phage tail-derived protein translocation system Afp, which causes enteric redmouth disease in salmonid fish species. Here we show that microinjection of the glycosyltransferase domain Afp18(G) into zebrafish embryos blocks cytokinesis, actin-dependent motility and cell blebbing, eventually abrogating gastrulation. In zebrafish ZF4 cells, Afp18(G) depolymerizes actin stress fibres by mono-O-GlcNAcylation of RhoA at tyrosine-34; thereby Afp18(G) inhibits RhoA activation by guanine nucleotide exchange factors, and blocks RhoA, but not Rac and Cdc42 downstream signalling. The crystal structure of tyrosine-GlcNAcylated RhoA reveals an open conformation of the effector loop distinct from recently described structures of GDP- or GTP-bound RhoA. Unravelling of the molecular mechanism of the toxin component Afp18 as glycosyltransferase opens new perspectives in studies of phage tail-derived protein translocation systems, which are preserved from archaea to human pathogenic prokaryotes.

PubMed: 26190758
DOI: 10.1038/ncomms8807

実験手法

X-RAY DIFFRACTION (2 Å)