β‐Lactamases (BLs) are important antibiotic‐resistance determinants that significantly compromise the efficacy of valuable β‐lactam antibacterial drugs. Thus, combinations with BL inhibitor were developed. Avibactam is the first non‐β‐lactam BL inhibitor introduced into clinical practice. Ceftazidime–avibactam represents one of the few last‐resort antibiotics available for the treatment of infections caused by near‐pandrug‐resistant bacteria. TRU‐1 is a chromosomally encoded AmpC‐type BL of Aeromonas enteropelogenes, related to the FOX‐type BLs and constitutes a good model for class C BLs. TRU‐1 crystals provided ultrahigh‐resolution diffraction data for the native enzyme and for its complex with avibactam. A comparison of the native and avibactam‐bound structures revealed new details in the conformations of residues relevant for substrate and/or inhibitor binding. Furthermore, a comparison of the TRU‐1 and Pseudomonas aeruginosa AmpC avibactam‐bound structures revealed two inhibitor conformations that were likely to correspond to two different states occurring during inhibitor carbamylation/recyclization.

中文翻译：

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C类β-内酰胺酶的原子分辨结构及其与阿维巴坦的复合物

β-内酰胺酶（BLs）是重要的抗生素耐药性决定因素，可显着损害宝贵的β-内酰胺抗菌药物的功效。因此，开发了与BL抑制剂的组合。阿维巴坦是首个引入临床的非β-内酰胺BL抑制剂。头孢他啶-阿维巴坦是可用于治疗由近乎耐药性细菌引起的感染的最后几种抗生素之一。TRU-1是肠气单胞菌的染色体编码AmpC型BL，与FOX型BL有关，是C类BL的良好模型。TRU-1晶体为天然酶及其与阿维巴坦的复合物提供了超高分辨率的衍射数据。天然和与阿维巴坦结合的结构的比较揭示了与底物和/或抑制剂结合相关的残基构象的新细节。此外，通过比较TRU-1和铜绿假单胞菌AmpC avibactam结合的结构，发现两种抑制剂构象可能与抑制剂氨甲酰化/再循环过程中发生的两种不同状态相对应。