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Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway
Open accessAbstract
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 non-hydrolysable ATP analog reveals subtle structural rearrangements upon nucleotide binding in the cleft between the N- and the C-terminal lobes. Remarkably, this new family of ELKs has a novel N-terminal domain topologically resembling the cystatin family of protease inhibitors. By interfacing with and restraining the mobility of the phosphate-binding region of the N-terminal lobe, Mak's unusual N-terminal domain might regulate its phosphotransfer activity and represents the most likely anchoring point for TreS, the upstream enzyme in the pathway. By completing the gallery of atomic-detail models of an essential pathway, this structure opens new avenues for the rational design of alternative anti-tubercular compounds.
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Metadata
- Authors
- Fraga, J., Maranha, A., Mendes, V., Pereira, P. J. B., Empadinhas, N., & Macedo-Ribeiro, S.
- Venue
- Scientific Reports
- Published
- 2015-01-26
- Volume
- 5
- Issue
- 1
- Pages
- 8026-8026
- ISSN
- 2045-2322 (ISSN-L)
- OpenAlex
- W1966729619
- Cited by
- 819
- References
- 46
- FWCI
- 12.26
- Type
- journal article
- Language
- en
- Open access
- gold
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