Igni18，一种来自嗜热古菌医院火球菌KIN4/I的新型金属水解酶：克隆、表达、纯化及X射线分析。
Igni18, a novel metallo-hydrolase from the hyperthermophilic archaeon Ignicoccus hospitalis KIN4/I: cloning, expression, purification and X-ray analysis.
作者信息
Kobus Stefanie, Perez-Garcia Pablo, Hoeppner Astrid, Holzscheck Nicholas, Kovacic Filip, Streit Wolfgang R, Jaeger Karl Erich, Chow Jennifer, Smits Sander H J
机构信息
Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany.
Department of Microbiology and Biotechnology, University of Hamburg, Ohnhorststrasse 18, 22609 Hamburg, Germany.
出版信息
Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):307-311. doi: 10.1107/S2053230X19002851. Epub 2019 Apr 2.
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, 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.
嗜热泉古菌医院火球菌KIN4/I至少拥有35个推定基因，这些基因编码属于α/β水解酶超家族的酶。其中一个基因igni18编码金属水解酶，已被克隆并在毕赤酵母中进行异源表达。所产生的酶以其催化活性形式进行了纯化。重组酶成功结晶，晶体衍射分辨率达到2.3 Å。该晶体属于R32空间群，晶胞参数为a = b = 67.42，c = 253.77 Å，α = β = 90.0，γ = 120.0°。据推测，不对称单元中包含一个Igni18单体。
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