8Z7M
The crystal structure of AFM-1
Summary for 8Z7M
| Entry DOI | 10.2210/pdb8z7m/pdb |
| Descriptor | Metallo-beta-lactamase type 2, ZINC ION (3 entities in total) |
| Functional Keywords | afm-1; metallo-beta-lactamase, metal binding protein |
| Biological source | Alcaligenes faecalis |
| Total number of polymer chains | 2 |
| Total formula weight | 51370.87 |
| Authors | |
| Primary citation | Niu, W.,Ti, R.,Li, D.,Dong, R.,Dong, J.,Ye, Y.,Xiao, Y.,Wang, Z. Structural insight into the subclass B1 metallo-beta-lactamase AFM-1. Biochem.Biophys.Res.Commun., 720:150102-150102, 2024 Cited by PubMed Abstract: The emergence of drug-resistant bacteria, facilitated by metallo-beta-lactamases (MBLs), presents a significant obstacle to the effective use of antibiotics in the management of clinical drug-resistant bacterial infections. AFM-1 is a MBL derived from Alcaligenes faecalis and shares 86% homology with the NDM-1 family. Both AFM-1 and NDM-1 demonstrate the ability to hydrolyze ampicillin and other β-lactam antibiotics, however, their substrate affinities vary, and the specific reason for this variation remains unknown. We present the high-resolution structure of AFM-1. The active center of AFM-1 binds two zinc ions, and the conformation of the key amino acid residues in the active center is in accordance with that of NDM-1. However, the substrate-binding pocket of AFM-1 is considerably smaller than that of NDM-1. Additionally, the mutation of amino acid residues in the Loop3 region, as compared to NDM-1, results in the formation of a dense hydrophobic patch comprised of hydrophobic amino acid residues in this area, which facilitates substrate binding. Our findings lay the foundation for understanding the molecular mechanism of AFM-1 with a high affinity for substrates and provide a novel theoretical foundation for addressing the issue of drug resistance caused by B1 MBLs. PubMed: 38759302DOI: 10.1016/j.bbrc.2024.150102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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