Analysis of crystalline and solution states of ligand-free spermidineN-acetyltransferase (SpeG) fromEscherichia coli

Autor: Steven Weigand, Wayne F. Anderson, Olga Kiryukhina, Ekaterina V. Filippova, Alan J. Wolfe
Rok vydání: 2019
Předmět:
Zdroj: Acta Crystallogr D Struct Biol
ISSN: 2059-7983
DOI: 10.1107/s2059798319006545
Popis: SpermidineN-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 fromVibrio choleraehas been characterized: while the monomer possesses a structural fold similar to those of other Gcn5-relatedN-acetyltransferase superfamily members, its dodecameric structure remains exceptional. In this paper, structural analyses of SpeG isolated fromEscherichia coliare described. LikeV. choleraeSpeG,E. coliSpeG forms dodecamers, as revealed by two crystal structures of the ligand-freeE. coliSpeG dodecamer determined at 1.75 and 2.9 Å resolution. Although bothV. choleraeSpeG andE. coliSpeG can adopt an asymmetric open dodecameric state, solution analysis showed that the oligomeric composition of ligand-freeE. coliSpeG differs from that of ligand-freeV. choleraeSpeG. 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.
Databáze: OpenAIRE
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