4BP0

Crystal structure of the closed form of Pseudomonas aeruginosa SPM-1

Summary for 4BP0

• Entry DOI: 10.2210/pdb4bp0/pdb
• Descriptor: METALLO-B-LACTAMASE, ZINC ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: hydrolase, metallo beta lactamase
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 4
• Total formula weight: 113347.72

Authors

McDonough, M.A.,Brem, J.,Schofield, C.J. (deposition date: 2013-05-22, release date: 2014-06-18, Last modification date: 2023-12-20)

Primary citation

Brem, J.,Struwe, W.B.,Rydzik, A.M.,Tarhonskaya, H.,Pfeffer, I.,Flashman, E.,van Berkel, S.S.,Spencer, J.,Claridge, T.D.,McDonough, M.A.,Benesch, J.L.,Schofield, C.J.
Studying the active-site loop movement of the Sao Paolo metallo-beta-lactamase-1
Chem Sci, 6:956-963, 2015

PubMed Abstract: Metallo-β-lactamases (MBLs) catalyse the hydrolysis of almost all β-lactam antibiotics. We report biophysical and kinetic studies on the São Paulo MBL (SPM-1), which reveal its Zn(ii) ion usage and mechanism as characteristic of the clinically important di-Zn(ii) dependent B1 MBL subfamily. Biophysical analyses employing crystallography, dynamic F NMR and ion mobility mass spectrometry, however, reveal that SPM-1 possesses loop and mobile element regions characteristic of the B2 MBLs. These include a mobile α3 region which is important in catalysis and determining inhibitor selectivity. SPM-1 thus appears to be a hybrid B1/B2 MBL. The results have implications for MBL evolution and inhibitor design.

PubMed: 25717359
DOI: 10.1039/c4sc01752h

Experimental method

X-RAY DIFFRACTION (2.24 Å)