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Structure paper

TitleMutation of an active site-adjacent residue in VIM indirectly dictates interactions with and blunts inhibition by D-captopril.
Journal, issue, pagesJ. Inorg. Biochem., Vol. 271, Page 112975-112975, Year 2025
Publish dateJul 28, 2024 (structure data deposition date)
AuthorsSilwal, S.B. / Wamsley, B. / Wang, Z. / Gung, B.W. / Nix, J.C. / Page, R.C.
External linksJ. Inorg. Biochem. / PubMed:40513263
MethodsX-ray diffraction
Resolution1.29 - 1.57 Å
Structure data

PDB-9cv1:
Crystal structure of the metallo-beta-lactamase VIM-15 with L-captopril
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

PDB-9cv2:
Crystal structure of the metallo-beta-lactamase VIM-20 with D-captopril
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-9cv3:
Crystal structure of the metallo-beta-lactamase VIM-20 with L-captopril
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-9cv4:
Crystal structure of the metallo-beta-lactamase VIM-31 with D-captopril
Method: X-RAY DIFFRACTION / Resolution: 1.36 Å

PDB-9cv5:
Crystal structure of the metallo-beta-lactamase VIM-31 with L-captopril
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-X8Z:
L-CAPTOPRIL / inhibitor, medication*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MCO:
1-(3-MERCAPTO-2-METHYL-PROPIONYL)-PYRROLIDINE-2-CARBOXYLIC ACID

ChemComp-ACT:
ACETATE ION

Source
  • pseudomonas aeruginosa (bacteria)
  • enterobacter cloacae (bacteria)
KeywordsHYDROLASE / metallo-beta-lactamase

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