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Igni18, a novel metallo-hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I: cloning, expression, purification and X-ray analysis.

ABSTRACT: The hyperthermophilic crenarchaeon Ignicoccus hospitalis KIN4/I possesses at least 35 putative genes encoding enzymes that belong to the ?/?-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 R32, with unit-cell parameters a = b = 67.42, c = 253.77?Å, ? = ? = 90.0, ? = 120.0°. It is suggested that it contains one monomer of Igni18 within the asymmetric unit.

SUBMITTER: Kobus S

PROVIDER: S-EPMC6450517 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Igni18, a novel metallo-hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I: cloning, expression, purification and X-ray analysis.

Kobus Stefanie S Perez-Garcia Pablo P Hoeppner Astrid A Holzscheck Nicholas N Kovacic Filip F Streit Wolfgang R WR Jaeger Karl Erich KE Chow Jennifer J Smits Sander H J SHJ

Acta crystallographica. Section F, Structural biology communications 20190402 Pt 4

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 R32, wit ...[more]

PMID: 30950832

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