Substrate-Induced Allosteric Change in the Quaternary Structure of the Spermidine N-Acetyltransferase SpeG

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Substrate-Induced Allosteric Change in the Quaternary Structure of the Spermidine N-Acetyltransferase SpeG

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作者：Ekaterina V. Filippova¹ ; Steven Weigand² ; Jerzy Osipiuk³ ; Olga Kiryukhina¹ ; Andrzej Joachimiak³ ; Wayne F. Anderson¹ ; ^{wf-anderson@northwestern.edu" class="auth_mail" title="E-mail the corresponding author}
关键词：AcCoA ; acetyl coenzyme A ; CoA ; coenzyme A ; MW ; molecular weight ; SEC ; size-exclusion chromatography ; MALS ; multi-angle light scattering ; FTS ; fluorescence thermal shift ; SAXS ; small-angle X-ray scattering ; EM ; electron microscopy ; PDB ; Protein Data Bank
刊名：Journal of Molecular Biology
出版年：2015
出版时间：6 November 2015
年：2015
卷：427
期：22
页码：3538-3553
全文大小：2673 K

文摘

•: Spermidine N-acetyltransferase (SpeG) in ligand-free form has multiple oligomeric forms in solution.
•: SpeG structure revealed a unique open dodecameric state.
•: Polyamine alters a shift from the asymmetric open state to the closed symmetric dodecameric state.

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