7EV5
Crystal structure of BLEG-1 B3 metallo-beta-lactamase
Summary for 7EV5
| Entry DOI | 10.2210/pdb7ev5/pdb |
| Descriptor | Lactamase_B domain-containing protein, ZINC ION, IODIDE ION, ... (4 entities in total) |
| Functional Keywords | b3 metallo-beta-lactamase, glyoxalase ii, metallo-hydrolase-like_mbl-fold protein, hydrolase |
| Biological source | Bacillus lehensis G1 |
| Total number of polymer chains | 1 |
| Total formula weight | 24651.15 |
| Authors | Au, S.X.,Muhd Noor, N.D.,Matsumura, H.,Rahman, R.N.Z.R.A.,Normi, Y.M. (deposition date: 2021-05-20, release date: 2021-09-08, Last modification date: 2023-11-29) |
| Primary citation | Au, S.X.,Dzulkifly, N.S.,Muhd Noor, N.D.,Matsumura, H.,Raja Abdul Rahman, R.N.Z.,Normi, Y.M. Dual Activity BLEG-1 from Bacillus lehensis G1 Revealed Structural Resemblance to B3 Metallo-beta-Lactamase and Glyoxalase II: An Insight into Its Enzyme Promiscuity and Evolutionary Divergence. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: Metallo-β-lactamases (MBLs) are class B β-lactamases from the metallo-hydrolase-like MBL-fold superfamily which act on a broad range of β-lactam antibiotics. A previous study on BLEG-1 (formerly called Bleg1_2437), a hypothetical protein from G1, revealed sequence similarity and activity to B3 subclass MBLs, despite its evolutionary divergence from these enzymes. Its relatedness to glyoxalase II (GLXII) raises the possibility of its enzymatic promiscuity and unique structural features compared to other MBLs and GLXIIs. This present study highlights that BLEG-1 possessed both MBL and GLXII activities with similar catalytic efficiencies. Its crystal structure revealed highly similar active site configuration to YcbL and GloB GLXIIs from , and L1 B3 MBL from . However, different from GLXIIs, BLEG-1 has an insertion of an active-site loop, forming a binding cavity similar to B3 MBL at the N-terminal region. We propose that BLEG-1 could possibly have evolved from GLXII and adopted MBL activity through this insertion. PubMed: 34502284DOI: 10.3390/ijms22179377 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.44 Å) |
Structure validation
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