7X78

L-fuculose 1-phosphate aldolase

Summary for 7X78

• Entry DOI: 10.2210/pdb7x78/pdb
• Descriptor: L-fuculose phosphate aldolase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: fuculose 1-phosphate aldolase, enzyme activity, klebsiella pneumoniae., lyase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 24079.75

Authors

Lou, X.,Zhang, Q.,Bartlam, M. (deposition date: 2022-03-09, release date: 2022-04-13, Last modification date: 2023-11-29)

Primary citation

Lou, X.,Zhang, J.,Liu, S.,Wang, R.,Li, W.,Liu, R.,Zhang, Q.,Bartlam, M.
Structural characterization of an L-fuculose-1-phosphate aldolase from Klebsiella pneumoniae.
Biochem.Biophys.Res.Commun., 607:15-19, 2022

PubMed Abstract: Fuculose phosphate aldolases play an important role in glycolysis and gluconeogenesis pathways. L-fuculose 1-phosphate aldolase catalyzes the reversible cleavage of L-fuculose 1-phosphate to DHAP and L-lactaldehyde. Class II aldolases found in bacteria are linked to pathogenesis of human pathogens, and have potential applications in the biosynthesis of carbohydrates and other chiral compounds. Here we report the structure of a putative L-fuculose 1-phosphate aldolase (KpFucA) from the nosocomial pathogen Klebsiella pneumoniae to 1.85 Å resolution. The enzyme crystallizes in space group P422 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis confirms that KpFucA is a tetramer in solution. A magnesium ion cofactor and sulfate ion were identified in the active pocket. Enzyme activity assays confirmed that KpFcuA has a strong preference for L-fuculose 1-phosphate as a substrate, but can also catalyze the cleavage of fructose-1,6-bisphosphate and glucose-6-phosphate. This work should provide a starting point for further investigation of the role of KpFucA in K. pneumoniae pathogenesis or in industrial applications.

PubMed: 35366538
DOI: 10.1016/j.bbrc.2022.03.127

Experimental method

X-RAY DIFFRACTION (1.85 Å)