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Igni18, a novel metallo‐hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I: cloning, expression, purification and X‐ray analysis
Author(s) -
Kobus Stefanie,
Perez-Garcia Pablo,
Hoeppner Astrid,
Holzscheck Nicholas,
Kovacic Filip,
Streit Wolfgang R.,
Jaeger Karl-Erich,
Chow Jennifer,
Smits Sander H. J.
Publication year - 2019
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/s2053230x19002851
Subject(s) - hydrolase , pichia pastoris , recombinant dna , cloning (programming) , biology , enzyme , gene , microbiology and biotechnology , molecular cloning , escherichia coli , biochemistry , gene expression , computer science , programming language
The hyperthermophilic crenarchaeon Ignicoccus hospitalis KIN4/I possesses at least 35 putative genes encoding enzymes that belong to the α/β‐hydrolase superfamily. One of those genes, the metallo‐hydrolase‐encoding igni18 , was cloned and heterologously expressed in Pichia pastoris . The enzyme produced was purified in its catalytically active form. The recombinant enzyme was successfully crystallized and the crystal diffracted to a resolution of 2.3 Å. The crystal belonged to space group R 32, with unit‐cell parameters a = b = 67.42, c = 253.77 Å, α = β = 90.0, γ = 120.0°. It is suggested that it contains one monomer of Igni18 within the asymmetric unit.