ArticleThe Journal of biological chemistry2012
The apo-structure of the low molecular weight protein-tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Learning millisecond protein dynamics from what is missing in NMR spectra.bioRxiv : the preprint server for biology · 2026Article
- The functions and inhibitors of protein tyrosine phosphatase B fromFrontiers in immunology · 2026Review
- Insights into Natural Products from Marine-Derived Fungi with Antimycobacterial Properties: Opportunities and Challenges.Marine drugs · 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
- MptpA Kinetics Enhanced by Allosteric Control of an Active Conformation.Journal of molecular biology · 2022Article
- Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- From infection niche to therapeutic target: the intracellular lifestyle ofMicrobiology (Reading, England) · 2021Review
- Article
- Substrate Activation of the Low-Molecular Weight Protein Tyrosine Phosphatase fromBiochemistry · 2020Article
- The domain architecture of PtkA, the first tyrosine kinase fromThe Journal of biological chemistry · 2018Article
- Protein tyrosine kinase, PtkA, is required for Mycobacterium tuberculosis growth in macrophages.Scientific reports · 2018Article
- Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Molecules (Basel, Switzerland) · 2017Review
- Characterization and 1.57 Å resolution structure of the key fire blight phosphatase AmsI from Erwinia amylovora.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Mycobacterium tuberculosis Serine/Threonine Protein Kinases.Microbiology spectrum · 2014Review
- Microbial protein-tyrosine kinases.The Journal of biological chemistry · 2014Review
- Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.Molecular and biochemical parasitology · 2014Article
- Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa.Journal of molecular biology · 2013Article
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Authors and funding
7 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-tyrosine phosphatases (PTPs) and protein-tyrosine kinases co-regulate cellular processes. In pathogenic bacteria, they are frequently exploited to act as key virulence factors for human diseases. Mycobacterium tuberculosis, the causative organism of tuberculosis, secretes a low molecular weight PTP (LMW-PTP), MptpA, which is required for its survival upon infection of host macrophages. Although there is otherwise no sequence similarity of LMW-PTPs to other classes of PTPs, the phosphate binding loop (P-loop) CX(5)R and the loop containing a critical aspartic acid residue (D-loop), required for the catalytic activity, are well conserved. In most high molecular weight PTPs, ligand binding to the P-loop triggers a large conformational reorientation of the D-loop, in which it moves ∼10 Å, from an "open" to a "closed" conformation. Until now, there have been no ligand-free structures of LMW-PTPs described, and hence the dynamics of the D-loop have remained largely unknown for these PTPs. Here, we present a high resolution solution NMR structure of the free form of the MptpA LMW-PTP. In the absence of ligand and phosphate ions, the D-loop adopts an open conformation. Furthermore, we characterized the binding site of phosphate, a competitive inhibitor of LMW-PTPs, on MptpA and elucidated the involvement of both the P- and D-loop in phosphate binding. Notably, in LMW-PTPs, the phosphorylation status of two well conserved tyrosine residues, typically located in the D-loop, regulates the enzyme activity. PtkA, the kinase complementary to MptpA, phosphorylates these two tyrosine residues in MptpA. We characterized the MptpA-PtkA interaction by NMR spectroscopy to show that both the P- and D-loop form part of the binding interface.
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