ArticleScientific reports2021
Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 17 citations in OpenAlex.
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- Chloroplast acetyltransferase GNAT2 acts as a redox-regulated switch for state transitions in tomato.Molecular horticulture · 2025Article
- Linalool exhibit antimicrobial ability againstCurrent research in microbial sciences · 2025Article
- Histone Modifications in the Anoxic Northern Crayfish, Faxonius virilis.Marine biotechnology (New York, N.Y.) · 2024Article
- High-quality genome of a novel Thermosynechococcaceae species from Namibia and characterization of its protein expression patterns at elevated temperatures.MicrobiologyOpen · 2024Article
- Enzyme-like Acyl Transfer Catalysis in a Bifunctional Organic Cage.Journal of the American Chemical Society · 2024Article
- Clinical Characteristics and Risk Factors for Infection and Death in Critically Ill Patients with Pulmonary Infection withInfection and drug resistance · 2024Article
- An acetyltransferase controls the metabolic flux in rubromycin polyketide biosynthesis by direct modulation of redox tailoring enzymes.Chemical science · 2022Article
- Genetic variation in symbiotic islands of natural variant strains of soybeanMicrobial genomics · 2022Article
- The role of altered protein acetylation in neurodegenerative disease.Frontiers in aging neuroscience · 2022Review
- Functional Analysis of Hypothetical Proteins ofBioinformatics and biology insights · 2022Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
General control non-repressible 5 (GCN5)-related N-acetyltransferases (GNATs) catalyse the acetylation of a diverse range of substrates, thereby orchestrating a variety of biological processes within prokaryotes and eukaryotes. GNAT enzymes can catalyze the transfer of an acetyl group from acetyl coenzyme A to substrates such as aminoglycoside antibiotics, amino acids, polyamines, peptides, vitamins, catecholamines, and large macromolecules including proteins. Although GNATs generally exhibit low to moderate sequence identity, they share a conserved catalytic fold and conserved structural motifs. In this current study we characterize the high-resolution X-ray crystallographic structure of a GNAT enzyme bound with acetyl-CoA from Elizabethkingia anophelis, an important multi-drug resistant bacterium. The tertiary structure is comprised of six α-helices and nine β-strands, and is similar with other GNATs. We identify a new and uncharacterized GNAT dimer interface, which is conserved in at least two other unpublished GNAT structures. This suggests that GNAT enzymes can form at least five different types of dimers, in addition to a range of other oligomers including trimer, tetramer, hexamer, and dodecamer assemblies. The high-resolution structure presented in this study is suitable for future in-silico docking and structure-activity relationship studies.
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