Summary for 5WQW
| Entry DOI | 10.2210/pdb5wqw/pdb |
| Descriptor | N-acetylglucosaminidase, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | autolysin, glycoside hydrolase 73 family, hydrolase |
| Biological source | Clostridium perfringens (strain 13 / Type A) |
| Total number of polymer chains | 1 |
| Total formula weight | 30948.74 |
| Authors | Tamai, E.,Sekiya, H.,Goda, E.,Makihata, N.,Maki, J.,Yoshida, H.,Kamitori, S. (deposition date: 2016-11-29, release date: 2016-12-07, Last modification date: 2024-03-20) |
| Primary citation | Tamai, E.,Sekiya, H.,Goda, E.,Makihata, N.,Maki, J.,Yoshida, H.,Kamitori, S. Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain FEBS Lett., 591:231-239, 2017 Cited by PubMed 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. PubMed: 27926788DOI: 10.1002/1873-3468.12515 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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