ArticleJournal of molecular biology2022
MptpA Kinetics Enhanced by Allosteric Control of an Active Conformation.
Article in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- NMR relaxation dispersion reveals an order of magnitude range of acid loop motions in protein tyrosine phosphatase 1B.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Identification of Key Residues in Allosteric Signaling of Photoactivated Adenylyl Cyclase.bioRxiv : the preprint server for biology · 2026Article
- Orchestrating function: Concerted dynamics, allostery, and catalysis in protein tyrosine phosphatases.Current opinion in structural biology · 2025Review
- Research progress on protein tyrosine phosphatase A from Mycobacterium tuberculosis.Frontiers in immunology · 2025Review
- Shikonin and Juglone InhibitBiotech (Basel (Switzerland)) · 2023Article
- MDiGest: A Python package for describing allostery from molecular dynamics simulations.The Journal of chemical physics · 2023Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Understanding allostery in the Mycobacterium tuberculosis low molecular weight protein tyrosine phosphatase (MptpA) is a subject of great interest since MptpA is one of two protein tyrosine phosphatases (PTPs) from the pathogenic organism Mycobacterium tuberculosis expressed during host cell infection. Here, we combine computational modeling with solution NMR spectroscopy and we find that Q75 is an allosteric site. Removal of the polar side chain of Q75 by mutation to leucine results in a cascade of events that reposition the acid loop over the active site and relocates the catalytic aspartic acid (D126) at an optimal position for proton donation to the leaving aryl group of the substrate and for subsequent hydrolysis of the thiophosphoryl intermediate. The computational analysis is consistent with kinetic data, and NMR spectroscopy, showing that the Q75L mutant exhibits enhanced reaction kinetics with similar substrate binding affinity. We anticipate that our findings will motivate further studies on the possibility that MptpA remains passivated during the chronic state of infection and increases its activity as part of the pathogenic life cycle of M. tuberculosis possibly via allosteric means.
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Registered trials
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