Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2010.06.011
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dc.titleStructural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis
dc.contributor.authorCheng, Z.
dc.contributor.authorHe, Y.-W.
dc.contributor.authorLim, S.C.
dc.contributor.authorQamra, R.
dc.contributor.authorWalsh, M.A.
dc.contributor.authorZhang, L.-H.
dc.contributor.authorSong, H.
dc.date.accessioned2014-10-27T08:40:38Z
dc.date.available2014-10-27T08:40:38Z
dc.date.issued2010-09
dc.identifier.citationCheng, Z., He, Y.-W., Lim, S.C., Qamra, R., Walsh, M.A., Zhang, L.-H., Song, H. (2010-09). Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis. Structure 18 (9) : 1199-1209. ScholarBank@NUS Repository. https://doi.org/10.1016/j.str.2010.06.011
dc.identifier.issn09692126
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101754
dc.description.abstractThe diffusible signal factor (DSF)-dependent quorum sensing (QS) system adopts a novel protein-protein interaction mechanism to autoregulate the production of signal DSF. Here, we present the crystal structures of DSF synthase RpfF and its complex with the REC domain of sensor protein RpfC. RpfF is structurally similarity to the members of the crotonase superfamily and contains an N-terminal α/β spiral core domain and a C-terminal α-helical region. Further structural and mutational analysis identified two catalytic glutamate residues, which is the conserved feature of the enoyl-CoA hydratases/dehydratases. A putative substrate-binding pocket was unveiled and the key roles of the residues implicated in substrate binding were verified by mutational analysis. The binding of the REC domain may lock RpfF in an inactive conformation by blocking the entrance of substrate binding pocket, thereby negatively regulating DSF production. These findings provide a structural model for the RpfC-RpfF interaction-mediated QS autoinduction mechanism. © 2010 Elsevier Ltd.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.str.2010.06.011
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.str.2010.06.011
dc.description.sourcetitleStructure
dc.description.volume18
dc.description.issue9
dc.description.page1199-1209
dc.description.codenSTRUE
dc.identifier.isiut000281836400016
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