8YOA
Crystal structure of endolytic transglycosylase MltG
Summary for 8YOA
| Entry DOI | 10.2210/pdb8yoa/pdb |
| Descriptor | Endolytic murein transglycosylase (2 entities in total) |
| Functional Keywords | mltg, lytic transglycosylase, peptidoglycan, membrane binding protein, membrane protein, lyase |
| Biological source | Mycobacteroides abscessus |
| Total number of polymer chains | 1 |
| Total formula weight | 37383.53 |
| Authors | |
| Primary citation | Lee, G.H.,Kim, S.,Kim, D.Y.,Han, J.H.,Lee, S.Y.,Lee, J.H.,Lee, C.S.,Park, H.H. Structure of MltG from Mycobacterium abscessus reveals structural plasticity between composed domains. Iucrj, 11:903-909, 2024 Cited by PubMed Abstract: MltG, a membrane-bound lytic transglycosylase, has roles in terminating glycan polymerization in peptidoglycan and incorporating glycan chains into the cell wall, making it significant in bacterial cell-wall biosynthesis and remodeling. This study provides the first reported MltG structure from Mycobacterium abscessus (maMltG), a superbug that has high antibiotic resistance. Our structural and biochemical analyses revealed that MltG has a flexible peptidoglycan-binding domain and exists as a monomer in solution. Further, the putative active site of maMltG was disclosed using structural analysis and sequence comparison. Overall, this study contributes to our understanding of the transglycosylation reaction of the MltG family, aiding the design of next-generation antibiotics targeting M. abscessus. PubMed: 39297240DOI: 10.1107/S2052252524008443 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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