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Tertiary structure and low-salt concentration adaptation mechanism of $$beta$$-lactamase from moderate halophile

Arai, Shigeki; Adachi, Motoyasu; Tamada, Taro; Tokunaga, Hiroko*; Ishibashi, Matsujiro*; Tokunaga, Masao*; Kuroki, Ryota

A high content of acidic residues of halophilic proteins may destabilize the structure of halophilic protein and take away an enzymatic function under low salt concentration. However, periplasmic proteins of moderate halophiles require adapting a wide range of salt concentration (0.5 M - saturated NaCl). In this study, we investigated the structural and functional characteristics of HaBLA derived from periplasm of a moderate halophile ${it Chromohalobacter}$ sp.560. By isothermal titration calorimetry, it was clarified that HaBLA hydrolyses penicillin G under 0 - 4 M NaCl. Moreover, by X-ray crystallographic analysis, we found the positive charges and the hydrophobic cluster near the entrance of the active site of HaBLA. These structural characteristics may attract penicillin G to the active site of HaBLA, which may participate in the low salt concentration adaptation of HaBLA.

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