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Function of your protein

MqnA is a chorismate dehydratase that has been studied in Streptomyces coelicolor. MqnA is important because it catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. MqnA folds like a venus flytrap and binds to Without the venus flytrap folding, the protein would be unable to access the binding site. Products of ScMqnA include 3-EPB and the presumed hydrolysis product, 3,4-dihydroxycyclohexa-1,5-dienoate (3,4-CHD). Menaquinone (MqnA) is of importance to study because it helps make molecules for the electron transport chain.

Biological relevance and broader implications

MqnA is important because it catalyzes the biosynthesis of menaquinone, which is an important player in the electron transport chain. According to Prasad et al. (2022), "Menaquinone serves as an electron carrier in the electron transport chain. Although some prokaryotes utilize ubiquinone solely, mycobacteria and most gram-positive bacteria produce menaquinone exclusively, and many gram-negative bacteria such as Escherichia coli switch from ubiquinone to menaquinone when grown under anaerobic conditions (2). In humans, menaquinone (vitamin K2) acts as a cosubstrate in the carboxylation of glutamic acids that leads to the activation of proteins essential for blood coagulation, control of cell growth, apoptosis, signal transduction, and calcium metabolism." Additionally, understanding the venus flytrap folding structure of this enzyme helps us understand the binding sites of similar enzymes.

Important amino acids

Amino acids involved in the catalytic triad for MqnA include N17, S86, and Y242. Other amino acids that help bind the main ligand through hydrophobic interactions include I13, N17, V18, P41, E42, V58, V84, S86, C87, S109, R110, T111, S112, I150, G151, F186, and Y242. A view of just the ligan is shown

Structural highlights

In terms of secondary structure, MqnA has both alpha helices and beta sheets present. In this , alpha helices are shown in red and beta sheets are shown in yellow. In our enzyme, there are two distinct lobes. These lobes are connected by linkers. Connected to the linkers on either lobe are beta sheets, followed by alpha helices. In terms of , we see two distinct lobes present in MqnA. In the image, it is clear just how much space is occupied by the atoms, making our catalytic triad tucked away and hidden. This demonstrates the importance of the venus flytrap fold that exposes our ligand for binding. Its change in conformation is absolutely vital for its function. The tertiary structure (folded protein structure) is held together by side chain interactions, such as that between SER108 and ARG111 on MqnA. The quaternary structure shows how closely packed the amino acids are, leaving little to no access without the venus flytrap fold.

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