Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2015.08.014
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dc.titleStructure of AcrH-AopB Chaperone-Translocator Complex Reveals a Role for Membrane Hairpins in Type III Secretion System Translocon Assembly
dc.contributor.authorNguyen, Van Sang
dc.contributor.authorJobichen, Chacko
dc.contributor.authorTan, Kang Wei
dc.contributor.authorTan, Yih Wan
dc.contributor.authorChan, Siew Leong
dc.contributor.authorRamesh, Karthik
dc.contributor.authorYuan, Yongming
dc.contributor.authorHong, Yunhan
dc.contributor.authorSeetharaman, Jayaraman
dc.contributor.authorLeung, Ka Yin
dc.contributor.authorSivaraman, J
dc.contributor.authorMok, Yu Keung
dc.date.accessioned2020-05-27T09:03:51Z
dc.date.available2020-05-27T09:03:51Z
dc.date.issued2015-11-03
dc.identifier.citationNguyen, 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.issn0969-2126
dc.identifier.issn1878-4186
dc.identifier.urihttps://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.isoen
dc.publisherCELL PRESS
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectCell Biology
dc.subjectCOILED-COIL DOMAINS
dc.subjectCOLICIN E1 CHANNEL
dc.subjectCRYSTAL-STRUCTURE
dc.subjectPSEUDOMONAS-AERUGINOSA
dc.subjectPROTEIN TRANSLOCATION
dc.subjectAEROMONAS-HYDROPHILA
dc.subjectFORMING DOMAIN
dc.subjectIA
dc.subjectPEPTIDE
dc.subjectSTATE
dc.typeArticle
dc.date.updated2020-05-27T07:46:39Z
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentBIOLOGY (NU)
dc.contributor.departmentDEPT OF CHEMISTRY
dc.description.doi10.1016/j.str.2015.08.014
dc.description.sourcetitleSTRUCTURE
dc.description.volume23
dc.description.issue11
dc.description.page2022-2031
dc.published.statePublished
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