3WIT

Crystal structure of the C-terminal region of VgrG1 from E. coli O157 EDL933

3WIT の概要

• エントリーDOI: 10.2210/pdb3wit/pdb
• 分子名称: Putative Vgr protein (2 entities in total)
• 機能のキーワード: triple-stranded beta-helix, all beta proteins, type 6 secretion system component, structural protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8618.48

構造登録者

Uchida, K.,Leiman, P.G.,Arisaka, F.,Kanamaru, S. (登録日: 2013-09-25, 公開日: 2013-12-18, 最終更新日: 2024-10-09)

主引用文献

Uchida, K.,Leiman, P.G.,Arisaka, F.,Kanamaru, S.
Structure and properties of the C-terminal beta-helical domain of VgrG protein from Escherichia coli O157
J.Biochem., 155:173-182, 2014

PubMed Abstract: The bacterial Type 6 secretion system (T6SS) translocates protein toxins (also called effectors) from the cytosol of a T6SS-carrying cell to a target cell by a syringe-like supramolecular complex resembling a contractile tail of bacteriophages. Valine-glycine repeat protein G (VgrG) proteins, which are the homologues of the gp27-gp5 (gene product) cell puncturing complex of bacteriophage T4, are considered to be located at the attacking tip of the bacterial T6SS apparatus. Here, we over-expressed six VgrG proteins from pathogenic Escherichia coli O157 and CFT073 strains. Purified VgrG1 of E. coli O157 and c3393 of E. coli CFT073 form trimer in solution and are rich in β-structure. We also solved the crystal structure of a trypsin-resistant C-terminal fragment of E. coli O157 VgrG1 (VgrG1C(G561)) at 1.95 Å resolution. VgrG1C(G561) forms a three-stranded antiparallel β-helix which is structurally similar to the β-helix domain of the central spike protein (gp138) of phi92 phage, indicating a possible evolutional relationship. Comparison of four different three-stranded β-helix proteins shows how their amino acid composition determines the protein fold.

PubMed: 24307403
DOI: 10.1093/jb/mvt109

実験手法

X-RAY DIFFRACTION (1.95 Å)