Structural insights into the assembly of the type III secretion needle complex

被引：299

作者：

Marlovits, TC

Kubori, T

Sukhan, A

Thomas, DR

Galán, JE

Unger, VM ^{[1
]}

机构：

[1] Yale Univ, Sch Med, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

[2] Yale Univ, Sch Med, Sect Microbial Pathogenet, New Haven, CT 06536 USA

[3] Brandeis Univ, Rosenstiel Basic Med Sci Res Ctr, Waltham, MA 02454 USA

来源：

SCIENCE | 2004年 / 306卷 / 5698期

关键词：

D O I：

10.1126/science.1102610

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Type III secretion systems (TTSSs) mediate translocation of virulence factors into host cells. We report the 17-angstrom resolution structures of a central component of Salmonella typhimurium TTSS, the needle complex, and its assembly precursor, the bacterial envelope-anchored base. Both the base and the fully assembled needle complex adopted multiple oligomeric states in vivo, and needle assembly was accompanied by recruitment of the protein PrgJ as a structural component of the base. Moreover, conformational changes during needle assembly created scaffolds for anchoring both PrgJ and the needle substructure and may provide the basis for substrate-specificity switching during type III secretion.

引用

页码：1040 / 1042

页数：3

共 14 条

[11] Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ [J].