3wr7

Crystal Structure of Spermidine Acetyltransferase from Escherichia coli

spinqualitylabelsall models 3wr7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wr7 is a 4 chain structure with sequence from Escherichia coli ly180. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: COA, SPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Spermidine acetyltransferase (SAT) from Escherichia coli, which catalyses the transfer of acetyl groups from acetyl-CoA to spermidine, is a key enzyme in controlling polyamine levels in prokaryotic cells. In this study, we determined the crystal structure of SAT in complex with spermidine (SPD) and CoA at 2.5A resolution. SAT is a dodecamer organized as a hexamer of dimers. The secondary structural element and folding topology of the SAT dimer resemble those of spermidine/spermine N(1)-acetyltransferase (SSAT), suggesting an evolutionary link between SAT and SSAT. However, the polyamine specificity of SAT is distinct from that of SSAT and is promiscuous. The SPD molecule is also located at the inter-dimer interface. The distance between SPD and CoA molecules is 13A. A deep, highly acidic, water-filled cavity encompasses the SPD and CoA binding sites. Structure-based mutagenesis and in-vitro assays identified SPD-bound residues, and the acidic residues lining the walls of the cavity are mostly essential for enzymatic activities. Based on mutagenesis and structural data, we propose an acetylation mechanism underlying promiscuous polyamine recognition for SAT. Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase.,Sugiyama S, Ishikawa S, Tomitori H, Niiyama M, Hirose M, Miyazaki Y, Higashi K, Murata M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Kashiwagi K, Igarashi K, Matsumura H Int J Biochem Cell Biol. 2016 Jul;76:87-97. doi: 10.1016/j.biocel.2016.05.003., Epub 2016 May 6. PMID:27163532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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