ArticleThe Journal of biological chemistry2016
Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Structural and Dynamic Insights into Acyl Carrier Protein upon Metal Binding and Acylation Revealed by NMR Spectroscopy and MD Simulations.International journal of molecular sciences · 2025Article
- Important Features for Protein Foldings in Two Acyl Carrier Proteins fromJournal of microbiology and biotechnology · 2024Article
- Structural properties and peptide ligand binding of the capsid homology domains of human Arc.Biochemistry and biophysics reports · 2021Article
- Deciphering the Binding Interactions betweenInternational journal of molecular sciences · 2021Article
- Structural Characterization of an ACP fromInternational journal of molecular sciences · 2020Article
- Article
- Disulfide Bond Engineering of an Endoglucanase fromInternational journal of molecular sciences · 2019Article
- Modular type I polyketide synthase acyl carrier protein domains share a common N-terminally extended fold.Scientific reports · 2019Article
- The Effect of Divalent Cations on the Thermostability of Type II Polyketide Synthase Acyl Carrier Proteins.AIChE journal. American Institute of Chemical Engineers · 2018Article
- Apigenin Impacts the Growth of the Gut Microbiota and Alters the Gene Expression of Enterococcus.Molecules (Basel, Switzerland) · 2017Article
- Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.Protein science : a publication of the Protein Society · 2017Article
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7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Enterococcus faecalis is a Gram-positive, commensal bacterium that lives in the gastrointestinal tracts of humans and other mammals. It causes severe infections because of high antibiotic resistance. E. faecalis can endure extremes of temperature and pH. Acyl carrier protein (ACP) is a key element in the biosynthesis of fatty acids responsible for acyl group shuttling and delivery. In this study, to understand the origin of high thermal stabilities of E. faecalis ACP (Ef-ACP), its solution structure was investigated for the first time. CD experiments showed that the melting temperature of Ef-ACP is 78.8 °C, which is much higher than that of Escherichia coli ACP (67.2 °C). The overall structure of Ef-ACP shows the common ACP folding pattern consisting of four α-helices (helix I (residues 3-17), helix II (residues 39-53), helix III (residues 60-64), and helix IV (residues 68-78)) connected by three loops. Unique Ef-ACP structural features include a hydrophobic interaction between Phe(45) in helix II and Phe(18) in the α1α2 loop and a hydrogen bonding between Ser(15) in helix I and Ile(20) in the α1α2 loop, resulting in its high thermal stability. Phe(45)-mediated hydrophobic packing may block acyl chain binding subpocket II entry. Furthermore, Ser(58) in the α2α3 loop in Ef-ACP, which usually constitutes a proline in other ACPs, exhibited slow conformational exchanges, resulting in the movement of the helix III outside the structure to accommodate a longer acyl chain in the acyl binding cavity. These results might provide insights into the development of antibiotics against pathogenic drug-resistant E. faecalis strains.
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