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The novel metallo-β-lactamase PNGM-1 from a deep-sea sediment metagenome: crystallization and X-ray crystallographic

Kwang Seung Park1, Myoung Ki Hong2, Jin Wan Jeon1

  • 1National Leading Research Laboratory of Drug Resistance Proteomics, Department of Biological Sciences, Myongji University, 116 Myongjiro, Yongin, Gyeonggido 17058, Republic of Korea.

Acta Crystallographica. Section F, Structural Biology Communications
|October 4, 2018
PubMed

Insights

Metallo-β-lactamases (MBLs) are enzymes that degrade antibiotics. Researchers crystallized PNGM-1, a B3 subclass MBL from deep-sea sediments, to understand its structure and function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Metallo-β-lactamases (MBLs) are critical in antibiotic resistance, hydrolyzing β-lactam antibiotics.
  • PNGM-1 is a unique B3 subclass MBL identified from ancient deep-sea sediment metagenomic libraries.

Purpose of the Study:

  • To overexpress, purify, and crystallize the PNGM-1 protein.
  • To determine the crystal structure of PNGM-1 for structural and functional analysis.

Main Methods:

  • Overexpression and purification of PNGM-1.
  • Crystallization of native and selenomethionine-substituted PNGM-1.
  • X-ray diffraction data collection and analysis.

Main Results:

  • PNGM-1 crystals diffracted to 2.10 Å (native) and 2.30 Å (selenomethionine-substituted).
  • Crystals belonged to the monoclinic space group P2₁.
  • Matthews coefficient calculations indicated 6-10 molecules in the asymmetric unit.

Conclusions:

  • The structural determination of PNGM-1 is underway.
  • This study provides a foundation for understanding novel MBLs predating the antibiotic era.
Keywords:
Edison Seamountantibiotic resistancedeep-sea sedimentmetagenomemetallo-β-lactamase

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