Background:IseA from Bacillus subtilis is an inhibitor protein against DL-endopeptidases including synthetic lethal autolysins. Results: We solved the solution structure of IseA using NMR. Titration with LytF DL-endopeptidase indicated interaction sites around the loop region. Conclusion: The IseA structure revealed a novel "hacksaw"-like fold with a characteristic inhibitory loop. Significance: The results suggest a new inhibition mechanism of IseA with a unique loop.
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