ArticleProtein science : a publication of the Protein Society2023
Allosteric inhibition of TEM-1 β lactamase: Microsecond molecular dynamics simulations provide mechanistic insights.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- The Evolving Landscape of Protein Allostery: From Computational and Experimental Perspectives.Journal of molecular biology · 2025Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Allosteric inhibition of TEM-1 β lactamase: Microsecond molecular dynamics simulations provide mechanistic insights.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
β-lactam antibiotics target DD-transpeptidases, enzymes that perform the last step of bacterial cell-wall synthesis. To block the antimicrobial activity of these antibiotics, bacteria have evolved lactamases that render them inert. Among these, TEM-1, a class A lactamase, has been extensively studied. In 2004, Horn et al. described a novel allosteric TEM-1 inhibitor, FTA, that binds distant from the TEM-1 orthosteric (penicillin-binding) pocket. TEM-1 has subsequently become a model for the study of allostery. In the present work, we perform molecular dynamics simulations of FTA-bound and FTA-absent TEM-1, totaling ~3 μS, that provide new insight into TEM-1 inhibition. In one of the simulations, bound FTA assumed a conformation different than that observed crystallographically. We provide evidence that the alternate pose is physiologically plausible and describe how it impacts our understanding of TEM-1 allostery.
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