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首页> 外文期刊>Acta crystallographica, Section D. Biological crystallography >Structure of a highly acidic beta-lactamase from the moderate halophile Chromohalobacter sp 560 and the discovery of a Cs+-selective binding site
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Structure of a highly acidic beta-lactamase from the moderate halophile Chromohalobacter sp 560 and the discovery of a Cs+-selective binding site

机译：中度嗜盐菌嗜盐菌560的高酸性β-内酰胺酶的结构和Cs +选择性结合位点的发现

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Environmentally friendly absorbents are needed for Sr2+ and Cs+, as the removal of the radioactive Sr2+ and Cs+ that has leaked from the Fukushima Nuclear Power Plant is one of the most important problems in Japan. Halophilic proteins are known to have many acidic residues on their surface that can provide specific binding sites for metal ions such as Cs+ or Sr2+. The crystal structure of a halophilic beta-lactamase from Chromohalobacter sp. 560 (HaBLA) was determined to resolutions of between 1.8 and 2.9 angstrom in space group P31 using X-ray crystallography. Moreover, the locations of bound Sr2+ and Cs+ ions were identified by anomalous X-ray diffraction. The location of one Cs+-specific binding site was identified in HaBLA even in the presence of a ninefold molar excess of Na+ (90 mM Na+/10 mM Cs+). From an activity assay using isothermal titration calorimetry, the bound Sr2+ and Cs+ ions do not significantly affect the enzymatic function of HaBLA. The observation of a selective and high-affinity Cs+-binding site provides important information that is useful for the design of artificial Cs+-binding sites that may be useful in the bioremediation of radioactive isotopes.
机译：Sr2 +和Cs +需要环保型吸收剂，因为从福岛核电站泄漏的放射性Sr2 +和Cs +的去除是日本最重要的问题之一。已知嗜盐蛋白质在其表面上具有许多酸性残基，这些酸性残基可以为金属离子（例如Cs +或Sr2 +）提供特定的结合位点。嗜盐杆菌属的嗜盐β-内酰胺酶的晶体结构。使用X射线晶体学，确定560（HaBLA）在空间群P31中的分辨率在1.8至2.9埃之间。此外，结合的Sr2 +和Cs +离子的位置通过异常X射线衍射确定。即使在存在9倍摩尔过量的Na +（90 mM Na + / 10 mM Cs +）的情况下，在HaBLA中也可以确定一个Cs +特异性结合位点的位置。从使用等温滴定量热法进行的活性分析中，结合的Sr2 +和Cs +离子不会显着影响HaBLA的酶功能。选择性和高亲和力的Cs +结合位点的观察提供了重要信息，可用于设计人工Cs +结合位点，这些位点可用于放射性同位素的生物修复。

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