7FCA

PfkB(Mycobacterium marinum)

Summary for 7FCA

• Entry DOI: 10.2210/pdb7fca/pdb
• Descriptor: Fructokinase, PfkB, GLYCEROL, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: pfkb, kinase, oxidoreductase, sandwich
• Biological source: Mycobacterium marinum (strain ATCC BAA-535 / M); More
• Total number of polymer chains: 6
• Total formula weight: 189705.56

Authors

Li, J.,Gao, B.,Ji, R. (deposition date: 2021-07-14, release date: 2021-08-04, Last modification date: 2023-11-29)

Primary citation

Gao, B.,Ji, R.,Li, Z.,Su, X.,Li, H.,Sun, Y.,Ji, C.,Gan, J.,Li, J.
Structural analysis and functional study of phosphofructokinase B (PfkB) from Mycobacterium marinum.
Biochem.Biophys.Res.Commun., 579:129-135, 2021

PubMed 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.

PubMed: 34597996
DOI: 10.1016/j.bbrc.2021.09.051

Experimental method

X-RAY DIFFRACTION (2.21 Å)