6CY6
Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Escherichia coli in complex with tris(hydroxymethyl)aminomethane.
Summary for 6CY6
| Entry DOI | 10.2210/pdb6cy6/pdb |
| Descriptor | Spermidine N(1)-acetyltransferase, CHLORIDE ION, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | speg, spermidine, gnat, n-acetyltransferase, structural genomics, center for structural genomics of infectious diseases, csgid, transferase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 23057.84 |
| Authors | Filippova, E.V.,Minasov, G.,Kiryukhina, O.,Anderson, W.F.,Satchell, K.J.F.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2018-04-04, release date: 2018-04-18, Last modification date: 2023-10-04) |
| Primary citation | Filippova, E.V.,Weigand, S.,Kiryukhina, O.,Wolfe, A.J.,Anderson, W.F. Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli. Acta Crystallogr D Struct Biol, 75:545-553, 2019 Cited by PubMed Abstract: 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 Å 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. PubMed: 31205017DOI: 10.1107/S2059798319006545 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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