Back

Molecular basis for the activation of the Fatty Acid Kinase complex of Staphylococcus aureus

Myers, M. J.; Xu, Z.; Ryan, B. J.; DeMars, Z. R.; Ridder, M. J.; Johnson, D. K.; Krute, C. N.; Flynn, T. S.; Kashipathy, M. M.; Battaile, K. P.; Schnicker, N. J.; Lovell, S.; Freudenthal, B. D.; Bose, J. L.

2024-03-19 microbiology
10.1101/2024.03.19.585040 bioRxiv
Show abstract

Gram-positive bacteria utilize a Fatty Acid Kinase (FAK) complex to harvest fatty acids from the environment. The complex, consisting of the fatty acid kinase, FakA, and an acyl carrier protein, FakB, is known to impact virulence and disease outcomes. However, FAKs structure and enzymatic mechanism remain poorly understood. Here, we used a combination of modeling, biochemical, and cell-based approaches to establish critical details of FAK activity. Solved structures of the apo and ligand-bound FakA kinase domain captured the protein state through ATP hydrolysis. Additionally, targeted mutagenesis of an understudied FakA Middle domain identified critical residues within a metal-binding pocket that contribute to FakA dimer stability and protein function. Regarding the complex, we demonstrated nanomolar affinity between FakA and FakB and generated computational models of the complexs quaternary structure. Together, these data provide critical insight into the structure and function of the FAK complex which is essential for understanding its mechanism.

Matching journals

The top 4 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.