1GA9

CRYSTAL STRUCTURE OF AMPC BETA-LACTAMASE FROM E. COLI COMPLEXED WITH NON-BETA-LACTAMASE INHIBITOR (2, 3-(4-BENZENESULFONYL-THIOPHENE-2-SULFONYLAMINO)-PHENYLBORONIC ACID)

Summary for 1GA9

• Entry DOI: 10.2210/pdb1ga9/pdb
• Related: 1C3B 2BLS 3BLS
• Descriptor: BETA-LACTAMASE, PHOSPHATE ION, 3-(4-BENZENESULFONYL-THIOPHENE-2-SULFONYLAMINO)-PHENYLBORONIC ACID, ... (5 entities in total)
• Functional Keywords: cephalosporinase, beta-lactamase, serine hydrolase, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00811
• Total number of polymer chains: 2
• Total formula weight: 80251.47

Authors

Tondi, D.,Powers, R.A.,Caselli, E.,Negri, M.C.,Blazquez, J.,Costi, M.P.,Shoichet, B.K. (deposition date: 2000-11-29, release date: 2001-07-25, Last modification date: 2024-10-09)

Primary citation

Tondi, D.,Powers, R.A.,Caselli, E.,Negri, M.C.,Blazquez, J.,Costi, M.P.,Shoichet, B.K.
Structure-based design and in-parallel synthesis of inhibitors of AmpC beta-lactamase.
Chem.Biol., 8:593-611, 2001

PubMed Abstract: Group I beta-lactamases are a major cause of antibiotic resistance to beta-lactams such as penicillins and cephalosporins. These enzymes are only modestly affected by classic beta-lactam-based inhibitors, such as clavulanic acid. Conversely, small arylboronic acids inhibit these enzymes at sub-micromolar concentrations. Structural studies suggest these inhibitors bind to a well-defined cleft in the group I beta-lactamase AmpC; this cleft binds the ubiquitous R1 side chain of beta-lactams. Intriguingly, much of this cleft is left unoccupied by the small arylboronic acids.

PubMed: 11410378
DOI: 10.1016/S1074-5521(01)00034-5

Experimental method

X-RAY DIFFRACTION (2.1 Å)