Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2015.08.014
Title: Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly
Authors: Nguyen, Van Sang 
Jobichen, Chacko 
Tan, Kang Wei 
Tan, Yih Wan
Chan, Siew Leong 
Ramesh, Karthik 
Yuan, Yongming 
Hong, Yunhan 
Seetharaman, Jayaraman
Leung, Ka Yin 
Sivaraman, J 
Mok, Yu Keung 
Keywords: Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Biophysics
Cell Biology
COILED-COIL DOMAINS
COLICIN E1 CHANNEL
CRYSTAL-STRUCTURE
PSEUDOMONAS-AERUGINOSA
PROTEIN TRANSLOCATION
AEROMONAS-HYDROPHILA
FORMING DOMAIN
IA
PEPTIDE
STATE
Issue Date: 3-Nov-2015
Publisher: CELL PRESS
Citation: Nguyen, Van Sang, Jobichen, Chacko, Tan, Kang Wei, Tan, Yih Wan, Chan, Siew Leong, Ramesh, Karthik, Yuan, Yongming, Hong, Yunhan, Seetharaman, Jayaraman, Leung, Ka Yin, Sivaraman, J, Mok, Yu Keung (2015-11-03). Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly. STRUCTURE 23 (11) : 2022-2031. ScholarBank@NUS Repository. https://doi.org/10.1016/j.str.2015.08.014
Abstract: © 2015 Elsevier Ltd. Type III secretion systems (T3SSs) are adopted by pathogenic bacteria for the transport of effector proteins into host cells through the translocon pore composed of major and minor translocator proteins. Both translocators require a dedicated chaperone for solubility. Despite tremendous efforts in the past, structural information regarding the chaperone-translocator complex and the topology of the translocon pore have remained elusive. Here, we report the crystal structure of the major translocator, AopB, from Aeromonas hydrophila AH-1 in complex with its chaperone, AcrH. Overall, the structure revealed unique interactions between the various interfaces of AopB and AcrH, with the N-terminal "molecular anchor" of AopB crossing into the "N-terminal arm" of AcrH. AopB adopts a novel fold, and its transmembrane regions form two pairs of helical hairpins. From these structural studies and associated cellular assays, we deduced the topology of the assembled T3SS translocon; both termini remain extracellular after membrane insertion.
Source Title: STRUCTURE
URI: https://scholarbank.nus.edu.sg/handle/10635/168529
ISSN: 0969-2126
1878-4186
DOI: 10.1016/j.str.2015.08.014
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