ArticleStructure (London, England : 1993)2021
Structural analysis of Mycobacterium tuberculosis M13 metalloprotease Zmp1 open states.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Dimerization and dynamics of human angiotensin-I converting enzyme revealed by cryo-EM and MD simulations.eLife · 2025Article
- Review of Recent Advances in Thiazolidin-4-One Derivatives as Promising Antitubercular Agents (2021-Present).Molecules (Basel, Switzerland) · 2025Review
- Host range expansion ofFrontiers in microbiology · 2025Article
- Novel marine metalloprotease-new approaches for inhibition of biofilm formation of Stenotrophomonas maltophilia.Applied microbiology and biotechnology · 2023Article
- Antimicrobial Resistance and Comparative Genomic Analysis ofAntibiotics (Basel, Switzerland) · 2022Article
- Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition.Nature communications · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Zinc metalloprotease 1 (Zmp1), a Mycobacterium tuberculosis 75 kDa secreted enzyme, mediates key stages of tuberculosis disease progression. The biological activity of Zmp1 presumably stems from its ability to degrade bacterium- and/or host-derived peptides. The crystal structures of Zmp1 and related M13 metalloproteases, such as neprilysin and endothelin-converting enzyme-1 were determined only in the closed conformation, which cannot capture substrates or release proteolytic products. Thus, the mechanisms of substrate binding and selectivity remain elusive. Here we report two open-state cryo-EM structures of Zmp1, revealed by our SAXS analysis to be the dominant states in solution. Our structural analyses reveal how ligand binding induces a conformational switch in four linker regions to drive the rigid body motion of the D1 and D2 domains, which form the sizable catalytic chamber. Furthermore, they offer insights into the catalytic cycle and mechanism of substrate recognition of M13 metalloproteases for future therapeutic innovations.
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Registered trials
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