Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jmb.2006.06.033
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dc.titleStructural Basis of the Sulphate Starvation Response in E. coli: Crystal Structure and Mutational Analysis of the Cofactor-binding Domain of the Cbl Transcriptional Regulator
dc.contributor.authorStec, E.
dc.contributor.authorWitkowska-Zimny, M.
dc.contributor.authorHryniewicz, M.M.
dc.contributor.authorNeumann, P.
dc.contributor.authorWilkinson, A.J.
dc.contributor.authorBrzozowski, A.M.
dc.contributor.authorVerma, C.S.
dc.contributor.authorZaim, J.
dc.contributor.authorWysocki, S.
dc.contributor.authorD. Bujacz, G.
dc.date.accessioned2014-10-27T08:40:38Z
dc.date.available2014-10-27T08:40:38Z
dc.date.issued2006-12-01
dc.identifier.citationStec, E., Witkowska-Zimny, M., Hryniewicz, M.M., Neumann, P., Wilkinson, A.J., Brzozowski, A.M., Verma, C.S., Zaim, J., Wysocki, S., D. Bujacz, G. (2006-12-01). Structural Basis of the Sulphate Starvation Response in E. coli: Crystal Structure and Mutational Analysis of the Cofactor-binding Domain of the Cbl Transcriptional Regulator. Journal of Molecular Biology 364 (3) : 309-322. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jmb.2006.06.033
dc.identifier.issn00222836
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101755
dc.description.abstractCbl is a member of the large family of LysR-type transcriptional regulators (LTTRs) common in bacteria and found also in Archaea and algal chloroplasts. The function of Cbl is required in Escherichia coli for expression of sulphate starvation-inducible (ssi) genes, associated with the biosynthesis of cysteine from organic sulphur sources (sulphonates). Here, we report the crystal structure of the cofactor-binding domain of Cbl (c-Cbl) from E. coli. The overall fold of c-Cbl is very similar to the regulatory domain (RD) of another LysR family member, CysB. The RD is composed of two subdomains enclosing a cavity, which is expected to bind effector molecules. We have constructed and analysed several full-length Cbl variants bearing single residue substitutions in the RD that affect cofactor responses. Using in vivo and in vitro transcription assays, we demonstrate that pssuE, a Cbl responsive promoter, is down-regulated not only by the cofactor, adenosine phosphosulphate (APS), but also by thiosulphate, and, that the same RD determinants are important for the response to both cofactors. We also demonstrate the effects of selected site-directed mutations on Cbl oligomerization and discuss these in the context of the structure. Based on the crystal structure and molecular modelling, we propose a model for the interaction of Cbl with adenosine phosphosulphate. © 2006 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jmb.2006.06.033
dc.sourceScopus
dc.subjectCbl regulator
dc.subjectcofactor-binding
dc.subjectcrystal structure
dc.subjectE. coli
dc.subjectLysR family
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.jmb.2006.06.033
dc.description.sourcetitleJournal of Molecular Biology
dc.description.volume364
dc.description.issue3
dc.description.page309-322
dc.description.codenJMOBA
dc.identifier.isiut000242436200009
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