3RX9

3D structure of SciN from an Escherichia coli Patotype

3RX9 の概要

• エントリーDOI: 10.2210/pdb3rx9/pdb
• 分子名称: Putative uncharacterized protein, SULFATE ION (3 entities in total)
• 機能のキーワード: transthyretin (1sn5) fold, lipoprotein, t6ss assembly, scis, lipid binding 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: 17071.32

構造登録者

Felisberto-Rodrigues, C.,Durand, E.,Aschtgen, M.-S.,Blangy, S.,Ortiz-Lombardia, M.,Douzy, B.,Cambillau, C.,Cascales, E. (登録日: 2011-05-10, 公開日: 2011-12-07, 最終更新日: 2024-04-03)

主引用文献

Felisberto-Rodrigues, C.,Durand, E.,Aschtgen, M.S.,Blangy, S.,Ortiz-Lombardia, M.,Douzi, B.,Cambillau, C.,Cascales, E.
Towards a Structural Comprehension of Bacterial Type VI Secretion Systems: Characterization of the TssJ-TssM Complex of an Escherichia coli Pathovar.
Plos Pathog., 7:e1002386-e1002386, 2011

PubMed Abstract: Type VI secretion systems (T6SS) are trans-envelope machines dedicated to the secretion of virulence factors into eukaryotic or prokaryotic cells, therefore required for pathogenesis and/or for competition towards neighboring bacteria. The T6SS apparatus resembles the injection device of bacteriophage T4, and is anchored to the cell envelope through a membrane complex. This membrane complex is composed of the TssL, TssM and TagL inner membrane anchored proteins and of the TssJ outer membrane lipoprotein. Here, we report the crystal structure of the enteroaggregative Escherichia coli Sci1 TssJ lipoprotein, a two four-stranded β-sheets protein that exhibits a transthyretin fold with an additional α-helical domain and a protruding loop. We showed that TssJ contacts TssM through this loop since a loop depleted mutant failed to interact with TssM in vitro or in vivo. Biophysical analysis of TssM and TssJ-TssM interaction suggest a structural model of the membrane-anchored outer shell of T6SS. Collectively, our results provide an improved understanding of T6SS assembly and encourage structure-aided drug design of novel antimicrobials targeting T6SS.

PubMed: 22102820
DOI: 10.1371/journal.ppat.1002386

実験手法

X-RAY DIFFRACTION (1.35 Å)