Abstract
GCN5-related N-acetyltransferases (GNATs) are the most widely distributed acetyltransferase systems among all three domains of life. GNATs appear to be involved in several key processes, including microbial antibiotic resistance, compacting eukaryotic DNA, controlling gene expression, and protein synthesis. Here, we report the crystal structure of a putative GNAT Ta0374 from Thermoplasma acidophilum, a hyperacidophilic bacterium, that has been determined in an apo-form, in complex with its natural ligand (acetyl coenzyme A), and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine. Sequence and structural analysis reveals that Ta0374 belongs to a novel protein family, PaiA, involved in the negative control of sporulation and degradative enzyme production. The crystal structure of Ta0374 confirms that it binds acetyl coenzyme A in a way similar to other GNATs and is capable of acetylating spermidine. Based on structural and docking analysis, it is expected that Glu53 and Tyr93 are key residues for recognizing spermidine. Additionally, we find that the purification His-Tag in the apo-form structure of Ta0374 prevents binding of acetyl coenzyme A in the crystal, though not in solution, and affects a chain-flip rotation of "motif A" which is the most conserved sequence among canonical acetyltransferases.
Original language | English (US) |
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Pages (from-to) | 2566-2577 |
Number of pages | 12 |
Journal | Proteins: Structure, Function and Bioinformatics |
Volume | 79 |
Issue number | 8 |
DOIs | |
State | Published - Aug 2011 |
Keywords
- Acetyl coenzyme A
- Degradative enzyme production
- GNAT acetyltransferase
- P-loop
- Pai operon
- Spermidine/spermine
- Sporulation
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
- Biochemistry
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Dive into the research topics of 'Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production'. Together they form a unique fingerprint.Datasets
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Structure of a putative n-acetyltransferase (ta0374) in complex with acetyl-coa from thermoplasma acidophilum
Filippova, E. V. (Contributor), Shuvalova, L. (Contributor), Minasov, G. (Contributor), Kiryukhina, O. (Contributor), Zhang, Y. (Contributor), Clancy, S. (Contributor), Radhakrishnan, I. (Contributor), Joachimiak, A. (Contributor) & Anderson, W. F. (Contributor), Protein Data Bank (PDB), Nov 11 2008
DOI: 10.2210/pdb3F0A/pdb, https://www.wwpdb.org/pdb?id=pdb_00003f0a
Dataset
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Crystal structure of paia acetyltransferase (ta0374) from thermoplasma acidophilum
Filippova, E. V. (Contributor), Shuvalova, L. (Contributor), Minasov, G. (Contributor), Kiryukhina, O. (Contributor), Zhang, Y. (Contributor), Clancy, S. (Contributor), Radhakrishnan, I. (Contributor), Joachimiak, A. (Contributor) & Anderson, W. F. (Contributor), Protein Data Bank (PDB), Nov 17 2009
DOI: 10.2210/pdb3K9U/pdb, https://www.wwpdb.org/pdb?id=pdb_00003k9u
Dataset
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Crystal structure of paia n-acetyltransferase from thermoplasma acidophilum in complex with coenzyme a
Filippova, E. V. (Contributor), Shuvalova, L. (Contributor), Minasov, G. (Contributor), Kiryukhina, O. (Contributor), Zhang, Y. (Contributor), Clancy, S. (Contributor), Radhakrishnan, I. (Contributor), Joachimiak, A. (Contributor) & Anderson, W. F. (Contributor), Protein Data Bank (PDB), Jul 28 2010
DOI: 10.2210/pdb3NE7/pdb, https://www.wwpdb.org/pdb?id=pdb_00003ne7
Dataset