6KBY
Crystal structure of a class C beta lactamase in complex with AMP
Summary for 6KBY
| Entry DOI | 10.2210/pdb6kby/pdb |
| Descriptor | Beta-lactamase, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | crystal structures, class c beta-lactamase, acyl-enzyme complex, amp, hydrolase |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 41060.54 |
| Authors | Bae, D.W.,Jung, Y.E.,An, Y.J.,Na, J.H.,Cha, S.S. (deposition date: 2019-06-26, release date: 2019-10-16, Last modification date: 2024-11-06) |
| Primary citation | Bae, D.W.,Jung, Y.E.,An, Y.J.,Na, J.H.,Cha, S.S. Structural Insights into Catalytic Relevances of Substrate Poses in ACC-1. Antimicrob.Agents Chemother., 63:-, 2019 Cited by PubMed Abstract: ACC-1 is a plasmid-encoded class C β-lactamase identified in clinical isolates of , , , and ACC-1-producing bacteria are susceptible to cefoxitin, whereas they are resistant to oxyimino cephalosporins. Here, we depict crystal structures of apo ACC-1, adenylylated ACC-1, and acylated ACC-1 complexed with cefotaxime and cefoxitin. ACC-1 has noteworthy structural alterations in the R2 loop, the Ω loop, and the Phe119 loop located along the active-site rim. The adenylate covalently bonded to the nucleophilic serine reveals a tetrahedral phosphorus mimicking the deacylation transition state. Cefotaxime in ACC-1 has a proper conformation for the substrate-assisted catalysis in that its C-4 carboxylate and N-5 nitrogen are adequately located to facilitate the deacylation reaction. In contrast, cefoxitin in ACC-1 has a distinct conformation, in which those functional groups cannot contribute to catalysis. Furthermore, the orientation of the deacylating water relative to the acyl carbonyl group in ACC-1 is unfavorable for nucleophilic attack. PubMed: 31451494DOI: 10.1128/AAC.01411-19 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.097 Å) |
Structure validation
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