AI Article Synopsis
- PfK B (phosphofructokinase B) is a member of the ribokinase family, catalyzing the conversion of fructose-6-phosphate to fructose-1,6-diphosphate, but its structure in Mycobacterium marinum was previously unclear.
- The study revealed that PfkB is monomeric in solution, contrasting with most enzymes in its family, and its crystal structure was determined at a resolution of 2.21 Å, showcasing two main domains.
- Structural analysis identified crucial residues (G236, A237, G238, D239) important for ATP catalysis and substrate binding, enhancing the understanding of glycolysis in M. marinum
Article Abstract
Phosphofructokinase B (PfkB) belongs to the ribokinase family, which uses the phosphorylated sugar as substrate, and catalyzes fructose-6-phosphate into fructose-1,6-diphosphate. However, the structural basis of Mycobacterium marinum PfkB is not clear. Here, we found that the PfkB protein was monomeric in solution, which was different from most enzymes in this family. The crystal structure of PfkB protein from M. marinum was solved at a resolution of 2.21 Å. The PfkB structure consists of two domains, a major three-layered α/β/α sandwich-like domain characteristic of the ribokinase-like superfamily, and a second domain composed of four-stranded β sheets. Structural comparison analysis suggested that residues G236, A237, G238, and D239 could be critical for ATP catalysis and substrate binding of PfkB. Our current work provides new insights into understanding the mechanism of the glycolysis in M. marinum.
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| http://dx.doi.org/10.1016/j.bbrc.2021.09.051 | DOI Listing |
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