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Arai, Shigeki; Yonezawa, Yasushi*; Okazaki, Nobuo*; Matsumoto, Fumiko*; Shibazaki, Chie; Shimizu, Rumi; Yamada, Mitsugu*; Adachi, Motoyasu; Tamada, Taro; Kawamoto, Masahide*; et al.
Acta Crystallographica Section D, 71(3), p.541 - 554, 2015/03
Times Cited Count:7 Percentile:50.44(Biochemical Research Methods)The crystal structure of halophilic -lactamase from sp.560 (HaBLA) was determined using X-ray crystallography. Moreover, the locations of bound Sr and Cs ions were identified by anomalous X-ray diffraction. The location of one Cs specific binding site was identified on HaBLA even in the presence of 9-fold molar excess of Na (90 mM Na /10 mM Cs). This Cs binding site is formed by two main-chain O atoms and an aromatic ring of a side chain of Trp. An aromatic ring of Trp interacts with Cs by the cation- interaction. The observation of a selective and high-affinity Cs binding site provides important information that is useful for designing artificial Cs binding sites useful in bioremediation of radioactive isotopes.
Arai, Shigeki; Adachi, Motoyasu; Kawamoto, Masahide*; Tokunaga, Hiroko*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota
no journal, ,
We attempted to discover the Cs and Sr binding sites on the halophilic -Lactamase (HaBLA) derived from sp.560 by the anomalous X-ray diffraction analysis. One Cs ions in the HaBLA crystal were identified by BL7 at SAGA-LS. Three Sr ions in the HaBLA crystal were identified by BL38B1 at SPring-8 and NW12A at Photon Factory. Discovered Cs binding site can bind Cs selectively from a solution containing Na/Cs = 90 mM/10 mM. This Cs binding site is formed by two main-chain O atoms and an aromatic ring of a side chain of Trp. An aromatic ring of Trp interacts with Cs by the cation- interaction. The observation of metal binding sites with relatively higher Cs selectivity provides important information that is useful for designing artificial Cs binding sites.