Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway
Universidade do Porto · University of Coimbra
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Abstract
A novel four-step pathway identified recently in mycobacteria channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan. The structures of three of the intervening enzymes - GlgB, GlgE, and TreS - were recently reported, providing the first templates for rational drug design. Here we describe the structural characterization of the fourth enzyme of the pathway, mycobacterial maltokinase (Mak), uncovering a eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases. The 1.15 Å structure of Mak in complex with a…
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Authors
6Topics & keywords
Topics
Keywords
- Phosphotransferases
- Transferase
- Kinase
- Biology
- Drug design
- Rational design
- Biochemistry
- Enzyme
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