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The novel metallo‐β‐lactamase PNGM‐1 from a deep‐sea sediment metagenome: crystallization and X‐ray crystallographic analysis
Author(s) -
Park Kwang Seung,
Hong Myoung-Ki,
Jeon Jin Wan,
Kim Ji Hwan,
Jeon Jeong Ho,
Lee Jung Hun,
Kim Tae Yeong,
Karim Asad Mustafa,
Malik Sumera Kausar,
Kang Lin-Woo,
Lee Sang Hee
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18012268
Subject(s) - monoclinic crystal system , crystallization , metagenomics , crystallography , chemistry , molecule , solvent , crystal structure , biochemistry , gene , organic chemistry
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 P 2 1 , with unit‐cell parameters a = 122, b = 83, c = 163 Å, β = 110°. Matthews coefficient ( V M ) calculations suggested the presence of 6–10 molecules in the asymmetric unit, corresponding to a solvent content of ∼31–58%. Structure determination is currently in progress.