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Literature summary for 2.3.1.48 extracted from

  • Shin, S.; Choe, J.
    Crystal structure of Pseudomonas aeruginosa N-acetyltransferase PA4534 (2017), Biochem. Biophys. Res. Commun., 487, 236-240 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene PA4534, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged enzyme in apoform and bound to acetyl-CoA, hanging drop vapor diffusion method, mixing of 8.5 mg/ml protein solution with reservoir solution contains 16% PEG 1000, 0.2 M calcium acetate, and 0.1 M Tris-HCl, pH 7.0, crystals of acetyl-CoA bound enzyme are obtained by mixing 0.49 mM protein and 0.7 mM acetyl-CoA and equilibrating with a well solution composed of 15% PEG 3350, 0.2 M ammonium citrate dibasic, and 0.1 M Tris-HCl, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.21 A and 1.62 A resolution, respectively, molecular replacement using the putative acetyltransferase YpeA structure (PDB ID 2PDO) as a search model, model building Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HVP3
-
-
Pseudomonas aeruginosa 1C Q9HVP3
-
-
Pseudomonas aeruginosa ATCC 15692 Q9HVP3
-
-
Pseudomonas aeruginosa CIP 104116 Q9HVP3
-
-
Pseudomonas aeruginosa DSM 22644 Q9HVP3
-
-
Pseudomonas aeruginosa JCM 14847 Q9HVP3
-
-
Pseudomonas aeruginosa LMG 12228 Q9HVP3
-
-
Pseudomonas aeruginosa PRS 101 Q9HVP3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through TEV protease, gel filtration, and ultrafiltration Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa ATCC 15692 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa 1C CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa PRS 101 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa DSM 22644 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa CIP 104116 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa LMG 12228 CoA + [protein]-N6-acetyl-L-lysine
-
?
acetyl-CoA + [protein]-L-lysine
-
Pseudomonas aeruginosa JCM 14847 CoA + [protein]-N6-acetyl-L-lysine
-
?

Subunits

Subunits Comment Organism
homodimer the dimer interface includes a domain swapping where strand beta7 of subunit A is located between strands beta5 and beta6 of subunit B, forming an antiparallel beta-sheet Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
N-acetyltransferase
-
Pseudomonas aeruginosa
PA4534
-
Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Pseudomonas aeruginosa

General Information

General Information Comment Organism
evolution the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86 Pseudomonas aeruginosa
additional information the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons Pseudomonas aeruginosa
physiological function GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate Pseudomonas aeruginosa