title: Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain.
abstract: 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 (AcpCD) at 1.76 Å resolution. AcpCD 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.
authors.affiliation: Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, Bunkyo-cho, Ehime, Japan.|Life Science Research Center and Faculty of Medicine, Kagawa University, Miki-cho, Kita-gun, Kagawa, Japan.
authors.forename: Eiji
authors.initials: E
authors.lastname: Tamai
authors.affiliation: Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, Bunkyo-cho, Ehime, Japan.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Sekiya
authors.affiliation: Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, Bunkyo-cho, Ehime, Japan.
authors.forename: Eri
authors.initials: E
authors.lastname: Goda
authors.affiliation: Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, Bunkyo-cho, Ehime, Japan.
authors.forename: Nahomi
authors.initials: N
authors.lastname: Makihata
authors.affiliation: Department of Infectious Disease, College of Pharmaceutical Science, Matsuyama University, Bunkyo-cho, Ehime, Japan.
authors.forename: Jun
authors.initials: J
authors.lastname: Maki
authors.affiliation: Life Science Research Center and Faculty of Medicine, Kagawa University, Miki-cho, Kita-gun, Kagawa, Japan.
authors.forename: Hiromi
authors.initials: H
authors.lastname: Yoshida
authors.affiliation: Life Science Research Center and Faculty of Medicine, Kagawa University, Miki-cho, Kita-gun, Kagawa, Japan.
authors.forename: Shigehiro
authors.initials: S
authors.lastname: Kamitori
mesh_terms: D000595:Amino Acid Sequence; D001433:Bacteriolysis; D020134:Catalytic Domain; D003016:Clostridium perfringens / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D016296:Mutagenesis / Q000235:genetics; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry* / Q000378:metabolism*; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D010457:Peptidoglycan; D009238:N-Acetylmuramoyl-L-alanine Amidase
keywords: X-ray structure; autolysin; glycoside hydrolase 73 family