Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.jsb.2009.12.024
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dc.titleThe crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket
dc.contributor.authorZhou, X.
dc.contributor.authorChua, T.K.
dc.contributor.authorTkaczuk, K.L.
dc.contributor.authorBujnicki, J.M.
dc.contributor.authorSivaraman, J.
dc.date.accessioned2014-06-17T10:15:26Z
dc.date.available2014-06-17T10:15:26Z
dc.date.issued2010-03
dc.identifier.citationZhou, X., Chua, T.K., Tkaczuk, K.L., Bujnicki, J.M., Sivaraman, J. (2010-03). The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket. Journal of Structural Biology 169 (3) : 277-285. ScholarBank@NUS Repository. https://doi.org/10.1016/j.jsb.2009.12.024
dc.identifier.issn10478477
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/67702
dc.description.abstractPolyamines are essential in all branches of life. Biosynthesis of spermidine, one of the most ubiquitous polyamines, is catalyzed by spermidine synthase (SpeE). Although the function of this enzyme from Escherichia coli has been thoroughly characterised, its structural details remain unknown. Here, we report the crystal structure of E. coli SpeE and study its interaction with the ligands by isothermal titration calorimetry and computational modelling. SpeE consists of two domains - a small N-terminal β-strand domain, and a C-terminal catalytic domain that adopts a canonical methyltransferase (MTase) Rossmann fold. The protein forms a dimer in the crystal and in solution. Structural comparison of E. coli SpeE to its homologs reveals that it has a large and unique substrate-binding cleft that may account for its lower amine substrate specificity. © 2009 Elsevier Inc. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.jsb.2009.12.024
dc.sourceScopus
dc.subjectAminopropyltransferase
dc.subjectCrystal structure
dc.subjectPolyamine synthase
dc.subjectRossmann fold
dc.subjectSpermidine synthase
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentDIVISION OF ENVIRONMENTAL SCIENCE & ENGG
dc.description.doi10.1016/j.jsb.2009.12.024
dc.description.sourcetitleJournal of Structural Biology
dc.description.volume169
dc.description.issue3
dc.description.page277-285
dc.description.codenJSBIE
dc.identifier.isiut000275296100003
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