ArticleActa crystallographica. Section F, Structural biology communications2018
The novel metallo-β-lactamase PNGM-1 from a deep-sea sediment metagenome: crystallization and X-ray crystallographic analysis.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. 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.
- ResFinderFG v2.0: a database of antibiotic resistance genes obtained by functional metagenomics.Nucleic acids research · 2023Article
- Structural Study of Metal Binding and Coordination in Ancient Metallo-β-Lactamase PNGM-1 Variants.International journal of molecular sciences · 2020Article
- Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-Emerging microbes & infections · 2019Article
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Abstract
Metallo-β-lactamases (MBLs) are present in major Gram-negative pathogens and environmental species, and pose great health risks because of their ability to hydrolyze the β-lactam rings of antibiotics such as carbapenems. PNGM-1 was the first reported case of a subclass B3 MBL protein that was identified from a metagenomic library from deep-sea sediments that predate the antibiotic era. In this study, PNGM-1 was overexpressed, purified and crystallized. Crystals of native and selenomethionine-substituted PNGM-1 diffracted to 2.10 and 2.30 Å resolution, respectively. Both the native and the selenomethionine-labelled PNGM-1 crystals belonged to the monoclinic space group P2
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