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 |
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Rok vydání: | 2019 |
Předmět: |
Models
Molecular Stereochemistry Crystallography X-Ray medicine.disease_cause 03 medical and health sciences chemistry.chemical_compound Acetyltransferases Structural Biology medicine Transferase Protein Structure Quaternary Escherichia coli 030304 developmental biology 0303 health sciences Escherichia coli K12 030306 microbiology Escherichia coli Proteins Research Papers Spermidine Dodecameric protein chemistry Acetylation Vibrio cholerae Polyamine acetylation Crystallization Polyamine |
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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