ArticleThe Journal of biological chemistry2016
Biochemical Roles for Conserved Residues in the Bacterial Fatty Acid-binding Protein Family.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Unexpected contribution of the Fak system and the thioesterase TesE to the growth and membrane physiology ofJournal of bacteriology · 2025Article
- Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.Nature structural & molecular biology · 2025Article
- Bacterial acquisition of host fatty acids has far-reaching implications on virulence.Microbiology and molecular biology reviews : MMBR · 2024Review
- Prophages divert Staphylococcus aureus defenses against host lipids.Journal of lipid research · 2024Article
- An inhibitory mechanism of AasS, an exogenous fatty acid scavenger: Implications for re-sensitization of FAS II antimicrobials.PLoS pathogens · 2024Article
- Syntrophic Interactions Ameliorate Arsenic Inhibition of Solvent-DechlorinatingEnvironmental science & technology · 2023Article
- The Phospholipase A1 Activity of Glycerol Ester Hydrolase (Geh) Is Responsible for Extracellular 2-12(mSphere · 2023Article
- Review
- Medium-Chain-Length Fatty Acid Catabolism in Cupriavidus necator H16: Transcriptome Sequencing Reveals Differences from Long-Chain-Length Fatty Acid β-Oxidation and Involvement of Several Homologous Genes.Applied and environmental microbiology · 2023Article
- Structure and mechanism for streptococcal fatty acid kinase (Fak) system dedicated to host fatty acid scavenging.Science advances · 2022Article
- Domain architecture and catalysis of the Staphylococcus aureus fatty acid kinase.The Journal of biological chemistry · 2022Article
- Branched chain fatty acid synthesis drives tissue-specific innate immune response and infection dynamics of Staphylococcus aureus.PLoS pathogens · 2021Article
- Staphylococcus aureus Lipase 3 (SAL3) is a surface-associated lipase that hydrolyzes short chain fatty acids.PloS one · 2021Article
- Article
- Article
- A fatty acid-binding protein ofThe Journal of biological chemistry · 2019Article
- Acyl-chain selectivity and physiological roles ofThe Journal of biological chemistry · 2019Article
- Staphylococcus aureus Utilizes Host-Derived Lipoprotein Particles as Sources of Fatty Acids.Journal of bacteriology · 2018Article
- Exogenous fatty acid metabolism in bacteria.Biochimie · 2017Review
- Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Fatty acid kinase (Fak) is a ubiquitous Gram-positive bacterial enzyme consisting of an ATP-binding protein (FakA) that phosphorylates the fatty acid bound to FakB. In Staphylococcus aureus, Fak is a global regulator of virulence factor transcription and is essential for the activation of exogenous fatty acids for incorporation into phospholipids. The 1.2-Å x-ray structure of S. aureus FakB2, activity assays, solution studies, site-directed mutagenesis, and in vivo complementation were used to define the functions of the five conserved residues that define the FakB protein family (Pfam02645). The fatty acid tail is buried within the protein, and the exposed carboxyl group is bound by a Ser-93-fatty acid carboxyl-Thr-61-His-266 hydrogen bond network. The guanidinium of the invariant Arg-170 is positioned to potentially interact with a bound acylphosphate. The reduced thermal denaturation temperatures of the T61A, S93A, and H266A FakB2 mutants illustrate the importance of the hydrogen bond network in protein stability. The FakB2 T61A, S93A, and H266A mutants are 1000-fold less active in the Fak assay, and the R170A mutant is completely inactive. All FakB2 mutants form FakA(FakB2)2 complexes except FakB2(R202A), which is deficient in FakA binding. Allelic replacement shows that strains expressing FakB2 mutants are defective in fatty acid incorporation into phospholipids and virulence gene transcription. These conserved residues are likely to perform the same critical functions in all bacterial fatty acid-binding proteins.
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