Please use this identifier to cite or link to this item: https://doi.org/10.1042/BJ20081588
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dc.titleIdentification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator
dc.contributor.authorJobichen, C.
dc.contributor.authorFernandis, A.Z.
dc.contributor.authorVelazquez-Campoy, A.
dc.contributor.authorLeung, K.Y.
dc.contributor.authorMok, Y.-K.
dc.contributor.authorWenk, M.R.
dc.contributor.authorSivaraman, J.
dc.date.accessioned2014-10-27T08:30:54Z
dc.date.available2014-10-27T08:30:54Z
dc.date.issued2009-06-01
dc.identifier.citationJobichen, C., Fernandis, A.Z., Velazquez-Campoy, A., Leung, K.Y., Mok, Y.-K., Wenk, M.R., Sivaraman, J. (2009-06-01). Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator. Biochemical Journal 420 (2) : 191-199. ScholarBank@NUS Repository. https://doi.org/10.1042/BJ20081588
dc.identifier.issn02646021
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100862
dc.description.abstractLipocalins are a broad family of proteins identified initially in eukaryotes and more recently in Gram-negative bacteria. The functions of lipocalin or lipid-binding proteins are often elusive and very diverse. Recently, we have determined the structure of GrlR (global regulator of LEE repressor), which plays a key role in the regulation of LEE (locus of enterocyte effacement) proteins. GrlR adopts a lipocalin-like fold that is composed of an eight-stranded β-barrel followed by an α-helix at the C-terminus. GrlR has a highly hydrophobic cavity region and could be a potential transporter of lipophilic molecules. To verify this hypothesis, we carried out structure-based analysis of GrlR, determined the structure of the lipid-GrlR complex and measured the binding of lipid to recombinant GrlR by ITC (isothermal titration calorimetry). In addition, we identified phosphatidylglycerol and phosphatidylethanolamine as the endogenously bound lipid species of GrlR using electrospray-ionization MS. Furthermore, we have shown that the lipid-binding property of GrlR is similar to that of its closest lipocalin structural homologue, β-lactoglobulin. Our studies demonstrate the hitherto unknown lipid-binding property of GrlR. © The Authors Journal compilation.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1042/BJ20081588
dc.sourceScopus
dc.subjectβ-barrel protein
dc.subjectGlobal regulator of LEE (locus of enterocyte effacement) repressor (Gr1R)
dc.subjectLipid
dc.subjectLipocalin
dc.subjectType III secretion system (T3SS)
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1042/BJ20081588
dc.description.sourcetitleBiochemical Journal
dc.description.volume420
dc.description.issue2
dc.description.page191-199
dc.description.codenBIJOA
dc.identifier.isiut000266649900006
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