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

被引：296
|
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
收藏
页码：1040 / 1042
页数：3
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