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TitleA beta-lactamase inhibitory protein mutant displays high potency and a broad inhibition profile due to an altered binding mode with beta-lactamases.
Journal, issue, pagesJ. Biol. Chem., Vol. 301, Page 110850-110850, Year 2025
Publish dateAug 12, 2025 (structure data deposition date)
AuthorsRivera, P. / Lu, S. / Ngango, D. / Sankaran, B. / Venkataram Prasad, B. / Palzkill, T.
External linksJ. Biol. Chem. / PubMed:41135675
MethodsX-ray diffraction
Resolution1.58 - 1.78 Å
Structure data

PDB-9q0a:
CTX-M-14 WT in complex with BLIP E73W
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-9q0b:
CTX-M-15 WT in complex with BLIP E73W
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

PDB-9q0c:
TEM-1 WT in complex with BLIP E73W
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • streptomyces clavuligerus (bacteria)
KeywordsHYDROLASE/PROTEIN BINDING / Antibiotic resistance / inhibition / BLIP / beta-lactamase / PROTEIN BINDING / HYDROLASE-PROTEIN BINDING complex / beta-lactamase inhibitory protein / inhibitory / protein / TEM

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