3K9U

Crystal structure of paia acetyltransferase (ta0374) from thermoplasma acidophilum

Summary for 3K9U

• Entry DOI: 10.2210/pdb3k9u/pdb
• Related: 3F0A 3FIX
• Descriptor: PaiA Acetyltransferase, CHLORIDE ION, NICKEL (II) ION, ... (6 entities in total)
• Functional Keywords: thermoplasma acidophilum, acetyltransferase, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, transferase
• Biological source: Thermoplasma acidophilum
• Total number of polymer chains: 2
• Total formula weight: 39481.76

Authors

Filippova, E.V.,Minasov, G.,Shuvalova, L.,Kiryukhina, O.,Joachimiak, A.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2009-10-16, release date: 2009-11-17, Last modification date: 2023-09-06)

Primary citation

Filippova, E.V.,Shuvalova, L.,Minasov, G.,Kiryukhina, O.,Zhang, Y.,Clancy, S.,Radhakrishnan, I.,Joachimiak, A.,Anderson, W.F.
Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.
Proteins, 79:2566-2577, 2011

PubMed 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.

PubMed: 21633970
DOI: 10.1002/prot.23062

Experimental method

X-RAY DIFFRACTION (2.3 Å)