6GMS

Solution NMR structure of the major type IV pilin PpdD from enterohemorrhagic Escherichia coli (EHEC)

6GMS の概要

• エントリーDOI: 10.2210/pdb6gms/pdb
• NMR情報: BMRB: 18823
• 分子名称: Prepilin peptidase-dependent protein D (1 entity in total)
• 機能のキーワード: type iv pilin adhesion ehec t4p, cell adhesion
• 由来する生物種: Escherichia coli O157:H7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14241.80

構造登録者

Amorim, G.C.,Bardiaux, B.,Luna-Rico, A.,Zeng, W.,Guilvout, I.,Egelman, E.,Nilges, M.,Francetic, O.,Izadi-Pruneyre, N. (登録日: 2018-05-28, 公開日: 2019-05-15, 最終更新日: 2024-11-13)

主引用文献

Bardiaux, B.,de Amorim, G.C.,Luna Rico, A.,Zheng, W.,Guilvout, I.,Jollivet, C.,Nilges, M.,Egelman, E.H.,Izadi-Pruneyre, N.,Francetic, O.
Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus.
Structure, 27:1082-1093.e5, 2019

PubMed Abstract: Bacterial type 4a pili are dynamic surface filaments that promote bacterial adherence, motility, and macromolecular transport. Their genes are highly conserved among enterobacteria and their expression in enterohemorrhagic Escherichia coli (EHEC) promotes adhesion to intestinal epithelia and pro-inflammatory signaling. To define the molecular basis of EHEC pilus assembly, we determined the structure of the periplasmic domain of its major subunit PpdD (PpdDp), a prototype of an enterobacterial pilin subfamily containing two disulfide bonds. The structure of PpdDp, determined by NMR, was then docked into the density envelope of purified EHEC pili obtained by cryoelectron microscopy (cryo-EM). Cryo-EM reconstruction of EHEC pili at ∼8 Å resolution revealed extremely high pilus flexibility correlating with a large extended region of the pilin stem. Systematic mutagenesis combined with functional and interaction analyses identified charged residues essential for pilus assembly. Structural information on exposed regions and interfaces between EHEC pilins is relevant for vaccine and drug discovery.

PubMed: 31056419
DOI: 10.1016/j.str.2019.03.021

実験手法

SOLUTION NMR