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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase
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Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase

机译：中子衍射研究破译细菌KDN9P磷酸酶中催化残基的质子化状态

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摘要

The enzyme 2-keto-3-deoxy-9-O-phosphonononic acid phosphatase (KDN9P phosphatase) functions in the pathway for the production of 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid, a sialic acid that is important for the survival of commensal bacteria in the human intestine. The enzyme is a member of the haloalkanoate dehalogenase superfamily and represents a good model for the active-site protonation state of family members. Crystals of approximate dimensions 1.5 x 1.0 x 1.0 mm were obtained in space group P2(1)2(1)2, with unit-cell parameters a = 83.1, b = 108.9, c = 75.7 angstrom. A complete neutron data set was collected from a medium-sized H/D-exchanged crystal at BIODIFF at the Heinz Maier-Leibnitz Zentrum (MLZ), Garching, Germany in 18 d. Initial refinement to 2.3 angstrom resolution using only neutron data showed significant density for catalytically important residues.
机译：酶2-酮-3-脱氧-9-O-膦酸磷酸酶（KDN9P磷酸酶）在产生2-酮-3-脱氧-D-甘油-D-半乳糖壬酸的途径中起作用酸对于人类肠道中的共生细菌的存活很重要。该酶是卤代链烷酸脱卤酶超家族的成员，并且代表家族成员的活性位质子化状态的良好模型。在空间组P2（1）2（1）2中获得了尺寸约为1.5 x 1.0 x 1.0 mm的晶体，其晶胞参数a = 83.1，b = 108.9，c = 75.7埃。在18 d时，从德国Heinz Maier-Leibnitz Zentrum（MLZ）的BIODIFF的中型H / D交换晶体收集了完整的中子数据集。仅使用中子数据初步精炼至2.3埃分辨率显示出重要催化残基的显着密度。

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