3o4f

Crystal Structure of Spermidine Synthase from E. coli

spinqualitylabelsall models 3o4f, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o4f is a 8 chain structure with sequence from Ecoli. This structure supersedes the now removed PDB entries 3adn and 3hh9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Gene: SPEE (ECOLI) Activity: Spermidine synthase, with EC number 2.5.1.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SPEE_ECOLI] Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Cadaverine (1,5-diaminopentane) and spermidine can replace putrescine as the propylamine acceptor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Polyamines 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 beta-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. The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket.,Zhou X, Chua TK, Tkaczuk KL, Bujnicki JM, Sivaraman J J Struct Biol. 2010 Mar;169(3):277-85. Epub 2010 Jan 4. PMID:20051267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Spermidine Synthase

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