6CY6

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

6CY6 の概要

• エントリーDOI: 10.2210/pdb6cy6/pdb
• 分子名称: Spermidine N(1)-acetyltransferase, CHLORIDE ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: speg, spermidine, gnat, n-acetyltransferase, structural genomics, center for structural genomics of infectious diseases, csgid, transferase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23057.84

構造登録者

Filippova, E.V.,Minasov, G.,Kiryukhina, O.,Anderson, W.F.,Satchell, K.J.F.,Joachimiak, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2018-04-04, 公開日: 2018-04-18, 最終更新日: 2023-10-04)

主引用文献

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

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: 31205017
DOI: 10.1107/S2059798319006545

実験手法

X-RAY DIFFRACTION (1.75 Å)