Please use this identifier to cite or link to this item:
https://doi.org/10.1016/j.str.2015.08.014
DC Field | Value | |
---|---|---|
dc.title | Structure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly | |
dc.contributor.author | Nguyen, Van Sang | |
dc.contributor.author | Jobichen, Chacko | |
dc.contributor.author | Tan, Kang Wei | |
dc.contributor.author | Tan, Yih Wan | |
dc.contributor.author | Chan, Siew Leong | |
dc.contributor.author | Ramesh, Karthik | |
dc.contributor.author | Yuan, Yongming | |
dc.contributor.author | Hong, Yunhan | |
dc.contributor.author | Seetharaman, Jayaraman | |
dc.contributor.author | Leung, Ka Yin | |
dc.contributor.author | Sivaraman, J | |
dc.contributor.author | Mok, Yu Keung | |
dc.date.accessioned | 2020-05-27T09:03:51Z | |
dc.date.available | 2020-05-27T09:03:51Z | |
dc.date.issued | 2015-11-03 | |
dc.identifier.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 | |
dc.identifier.issn | 0969-2126 | |
dc.identifier.issn | 1878-4186 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/168529 | |
dc.description.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. | |
dc.language.iso | en | |
dc.publisher | CELL PRESS | |
dc.source | Elements | |
dc.subject | Science & Technology | |
dc.subject | Life Sciences & Biomedicine | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biophysics | |
dc.subject | Cell Biology | |
dc.subject | COILED-COIL DOMAINS | |
dc.subject | COLICIN E1 CHANNEL | |
dc.subject | CRYSTAL-STRUCTURE | |
dc.subject | PSEUDOMONAS-AERUGINOSA | |
dc.subject | PROTEIN TRANSLOCATION | |
dc.subject | AEROMONAS-HYDROPHILA | |
dc.subject | FORMING DOMAIN | |
dc.subject | IA | |
dc.subject | PEPTIDE | |
dc.subject | STATE | |
dc.type | Article | |
dc.date.updated | 2020-05-27T07:46:39Z | |
dc.contributor.department | DEPT OF BIOLOGICAL SCIENCES | |
dc.contributor.department | BIOLOGY (NU) | |
dc.contributor.department | DEPT OF CHEMISTRY | |
dc.description.doi | 10.1016/j.str.2015.08.014 | |
dc.description.sourcetitle | STRUCTURE | |
dc.description.volume | 23 | |
dc.description.issue | 11 | |
dc.description.page | 2022-2031 | |
dc.published.state | Published | |
Appears in Collections: | Staff Publications Elements |
Show simple item record
Files in This Item:
File | Description | Size | Format | Access Settings | Version | |
---|---|---|---|---|---|---|
Crystal structrure of AcrH-AopB complex_31 Aug_supplemental.pdf | Supporting information | 516.13 kB | Adobe PDF | OPEN | Pre-print | View/Download |
Crystal structure of AcrH-AopB complex_31 Aug_S.pdf | Accepted version | 1.4 MB | Adobe PDF | OPEN | Pre-print | View/Download |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.