6cy6 | pdb_00006cy6

Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Escherichia coli in complex with tris(hydroxymethyl)aminomethane.

spinqualitylabelsall models 6cy6, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cy6 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: CL, MPD, MRD, NA, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATDA_ECOLI Regulates polyamine concentration by their degradation. Acts on spermidine, forming N(1)- and N(8)-acetylspermidine. Publication Abstract from PubMed Spermidine N-acetyltransferase (SpeG) transfers an acetyl group from acetyl-coenzyme A to an N-terminal amino group of intracellular spermidine. This acetylation inactivates spermidine, reducing the polyamine toxicity that tends to occur under certain chemical and physical stresses. The structure of the SpeG protein from Vibrio cholerae has been characterized: while the monomer possesses a structural fold similar to those of other Gcn5-related N-acetyltransferase superfamily members, its dodecameric structure remains exceptional. In this paper, structural analyses of SpeG isolated from Escherichia coli are described. Like V. cholerae SpeG, E. coli SpeG forms dodecamers, as revealed by two crystal structures of the ligand-free E. coli SpeG dodecamer determined at 1.75 and 2.9 A resolution. Although both V. cholerae SpeG and E. coli SpeG can adopt an asymmetric open dodecameric state, solution analysis showed that the oligomeric composition of ligand-free E. coli SpeG differs from that of ligand-free V. cholerae SpeG. Based on these data, it is proposed that the equilibrium balance of SpeG oligomers in the absence of ligands differs from one species to another and thus might be important for SpeG function. Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli.,Filippova EV, Weigand S, Kiryukhina O, Wolfe AJ, Anderson WF Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):545-553. doi:, 10.1107/S2059798319006545. Epub 2019 May 28. PMID:31205017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Spermidine/spermine N-acetyltransferase

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