2N50

Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis

Summary for 2N50

• Entry DOI: 10.2210/pdb2n50/pdb
• Related: 2N4Z
• NMR Information: BMRB: 25688
• Descriptor: Acyl carrier protein (1 entity in total)
• Functional Keywords: acyl carrier protein, enterococcus faecalis, fatty acid synthase, biosynthetic protein
• Biological source: Enterococcus faecalis V583
• Cellular location: Cytoplasm : Q82ZE9
• Total number of polymer chains: 1
• Total formula weight: 8840.64

Authors

Park, Y.,Jung, M.,Song, H.,Jeong, K.,Kim, Y. (deposition date: 2015-07-02, release date: 2015-12-09, Last modification date: 2024-05-15)

Primary citation

Park, Y.G.,Jung, M.C.,Song, H.,Jeong, K.W.,Bang, E.,Hwang, G.S.,Kim, Y.
Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis.
J. Biol. Chem., 291:1692-1702, 2016

PubMed 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.

PubMed: 26631734
DOI: 10.1074/jbc.M115.674408

Experimental method

SOLUTION NMR