Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly

Van Sang Nguyen; Chacko Jobichen; Kang Wei Tan; Yih Wan Tan; Siew Leong Chan; Karthik Ramesh; Yongming Yuan; Yunhan Hong; Jayaraman Seetharaman; Ka Yin Leung; J. Sivaraman; Yu Keung Mok

doi:10.1016/j.str.2015.08.014

Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly

Van Sang Nguyen, Chacko Jobichen, Kang Wei Tan, Yih Wan Tan, Siew Leong Chan, Karthik Ramesh, Yongming Yuan, Yunhan Hong, Jayaraman Seetharaman, Ka Yin Leung, J. Sivaraman, Yu Keung Mok^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	2022-2031
Number of pages	10
Journal	Structure
Volume	23
Issue number	11
DOIs	https://doi.org/10.1016/j.str.2015.08.014
State	Published - 3 Nov 2015
Externally published	Yes

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Nguyen, V. S., Jobichen, C., Tan, K. W., Tan, Y. W., Chan, S. L., Ramesh, K., Yuan, Y., Hong, Y., Seetharaman, J., Leung, K. Y., Sivaraman, J., & Mok, Y. K. (2015). 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. https://doi.org/10.1016/j.str.2015.08.014

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title = "Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly",

abstract = "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.",

author = "Nguyen, {Van Sang} and Chacko Jobichen and Tan, {Kang Wei} and Tan, {Yih Wan} and Chan, {Siew Leong} and Karthik Ramesh and Yongming Yuan and Yunhan Hong and Jayaraman Seetharaman and Leung, {Ka Yin} and J. Sivaraman and Mok, {Yu Keung}",

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year = "2015",

month = nov,

day = "3",

doi = "10.1016/j.str.2015.08.014",

language = "英语",

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T1 - Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly

AU - Nguyen, Van Sang

AU - Jobichen, Chacko

AU - Tan, Kang Wei

AU - Tan, Yih Wan

AU - Chan, Siew Leong

AU - Ramesh, Karthik

AU - Yuan, Yongming

AU - Hong, Yunhan

AU - Seetharaman, Jayaraman

AU - Leung, Ka Yin

AU - Sivaraman, J.

AU - Mok, Yu Keung

PY - 2015/11/3

Y1 - 2015/11/3

N2 - 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.

AB - 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.

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DO - 10.1016/j.str.2015.08.014

M3 - 文章

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AN - SCOPUS:84946137312

SN - 0969-2126

VL - 23

SP - 2022

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JO - Structure

JF - Structure

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ER -

Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly

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