What is it about?
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 selenomethionine-labelled PNGM-1 crystals belong to the monoclinic space group P21, with unit–cell parameters as follows: a = 122, b = 83, c = 163 Å, β = 110°. Matthews coefficient (VM) calculations suggested the presence of 6–10 molecules in the asymmetric unit, corresponding to a solvent content of ~31–58%.
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Why is it important?
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 the antibiotics such as carbapenems. PNGM-1 was the first reported case of a subclass B3 MBL protein that was identified from a metagenomic library of deep-sea sediments that predated the antibiotic era.
Perspectives
Metallo-β-lactamases (MBLs) may hydrolyze the β-lactam rings of antibiotics. PNGM-1 is a subclass B3 deep-sea sediment MBL that predates the antibiotic era. Crystals of native and selenomethionine-substituted PNGM-1 diffracted to 2.1 and 2.3 Å resolution, respectively. They belonged to space group P21 and probably contain 6-10 molecules in the crystallographic asymmetric unit.
Professor Sang Hee Lee
Myongji University
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This page is a summary of: The novel metallo-β-lactamase PNGM-1 from a deep-sea sediment metagenome: crystallization and X-ray crystallographic analysis, Acta Crystallographica Section F Structural Biology Communications, September 2018, International Union of Crystallography,
DOI: 10.1107/s2053230x18012268.
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