7Y4H
AcvX from Actinomadura viridis that exhibits deglycosylation activity on lobophorins
Summary for 7Y4H
| Entry DOI | 10.2210/pdb7y4h/pdb |
| Descriptor | AcvX (2 entities in total) |
| Functional Keywords | actinomadura viridis, hydrolase, lobophorin, deglycosylation |
| Biological source | Actinomadura viridis |
| Total number of polymer chains | 1 |
| Total formula weight | 37492.11 |
| Authors | Tan, B.,Zhang, L.P.,Zhang, C.S. (deposition date: 2022-06-14, release date: 2023-05-24, Last modification date: 2024-04-03) |
| Primary citation | Tan, B.,Zhang, L.,Zhang, Q.,Chen, S.,Xiong, W.,Zhu, Y.,Zhang, C. A Widespread Glycosidase Confers Lobophorin Resistance and Host-Dependent Structural Diversity. Angew.Chem.Int.Ed.Engl., 62:e202302043-e202302043, 2023 Cited by PubMed Abstract: Identifying new environmental resistance determinants is significant to combat rising antibiotic resistance. Herein we report the unexpected correlation of a lobophorin (LOB) resistance-related glycosidase KijX with the host-dependent chemical diversity of LOBs, by a process of glycosylation, deglycosylation and reglycosylation. KijX homologues are widespread among bacteria, archaea and fungi, and encode the same glycohydrolytic activity on LOBs. The crystal structure of AcvX (a KijX homologue) shows a similar fold to that of the glycoside hydrolase family 113 and a special negatively charged groove to accommodate and deglycosylate LOBs. Antagonistic assays indicate kijX as a defense weapon of actinomycetes to combat LOB producers in environment, reflecting an elegant coevolution relationship. Our study provides insight into the KijX-related glycosidases as preexisting resistance determinants and represents an example of resistance genes accidentally integrated into natural product assembly. PubMed: 37076762DOI: 10.1002/anie.202302043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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