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

页码：1040 / 1042

页数：3

共 50 条

[31] Type III secretion systems and bacterial flagella: Insights into their function from structural similarities
Blocker, A
Komoriya, K
Aizawa, S
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (06) : 3027 - 3030
[32] Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG
Sun, Ping
Tropea, Joseph E.
Austin, Brian P.
Cherry, Scott
Waugh, David S.
JOURNAL OF MOLECULAR BIOLOGY, 2008, 377 (03) : 819 - 830
[33] Structural insights into assembly of transcription preinitiation complex
Chen, Xizi
Xu, Yanhui
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2022, 75
[34] Protein refolding is required for assembly of the type three secretion needle
Ömer Poyraz
Holger Schmidt
Karsten Seidel
Friedmar Delissen
Christian Ader
Hezi Tenenboim
Christian Goosmann
Britta Laube
Andreas F Thünemann
Arturo Zychlinsky
Marc Baldus
Adam Lange
Christian Griesinger
Michael Kolbe
Nature Structural & Molecular Biology, 2010, 17 : 788 - 792
[35] Protein refolding is required for assembly of the type three secretion needle
Poyraz, Oemer
Schmidt, Holger
Seidel, Karsten
Delissen, Friedmar
Ader, Christian
Tenenboim, Hezi
Goosmann, Christian
Laube, Britta
Thuenemann, Andreas F.
Zychlinsky, Arturo
Baldus, Marc
Lange, Adam
Griesinger, Christian
Kolbe, Michael
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2010, 17 (07) : 788 - U26
[36] Structural and Functional Insights into the Pilotin-Secretin Complex of the Type II Secretion System
Gu, Shuang
Rehman, Saima
Wang, Xiaohui
Shevchik, Vladimir E.
Pickersgill, Richard W.
PLOS PATHOGENS, 2012, 8 (02)
[37] Structural insights into the Type II secretion nanomachine
McLaughlin, Lorraine S.
Haft, Rembrandt J. F.
Forest, Katrina T.
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2012, 22 (02) : 208 - 216
[38] Structural insights into the control of type three secretion
Abrusci, P.
Johnson, S.
Roversi, P.
McDowell, M.
Lea, S. M.
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2011, 40 : 142 - 142
[39] Deciphering the assembly of the Yersinia type III secretion injectisome
Diepold, Andreas
Amstutz, Marlise
Abel, Soeren
Sorg, Isabel
Jenal, Urs
Cornelis, Guy R.
EMBO JOURNAL, 2010, 29 (11): : 1928 - 1940
[40] Assembly and architecture of the type III secretion sorting platform
Soto, Eduardo
Galan, Jorge E.
Lara-Tejero, Marfa
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2022, 119 (51)

← 1 2 3 4 5 →