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Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain
Author(s) -
Tamai Eiji,
Sekiya Hiroshi,
Goda Eri,
Makihata Nahomi,
Maki Jun,
Yoshida Hiromi,
Kamitori Shigehiro
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12515
Subject(s) - autolysin , clostridium perfringens , hydrolase , glycoside hydrolase , chemistry , substrate (aquarium) , biochemistry , autolysis (biology) , peptidoglycan , cell wall , enzyme , stereochemistry , biology , bacteria , ecology , genetics
Bacterial autolysins can partially hydrolyze cell wall peptidoglycans into small sections to regulate cell separation/division and the growth phase. Clostridium perfringens autolysin (Acp) has an N‐terminal cell wall‐binding domain and a C‐terminal catalytic domain with glucosaminidase activity that belongs to the glycoside hydrolase 73 family. Here, we determined the X‐ray structure of the Acp catalytic domain (Acp CD ) at 1.76 Å resolution. Acp CD has a unique crescent‐shaped structure, forming a deep groove for substrate‐binding at the center of the protein. The modeling study of the enzyme/substrate complex demonstrated that the length of the substrate‐binding groove is closely related to the glucosaminidase activity. Mutagenesis analysis showed that AcpCD likely adopts a neighboring‐group mechanism for the catalytic reaction.