3P98
The crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrate
Summary for 3P98
| Entry DOI | 10.2210/pdb3p98/pdb |
| Related | 1BTL 1HTZ 1LHY 1LI9 1M40 1ZG4 |
| Descriptor | Beta-lactamase TEM-72, CITRIC ACID, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | aba-sandwich, beta-lactamase, hydrolase |
| Biological source | Morganella morganii (Proteus morganii) |
| Total number of polymer chains | 2 |
| Total formula weight | 63702.95 |
| Authors | Docquier, J.D.,Benvenuti, M.,Calderone, V.,Rossolini, G.M.,Mangani, S. (deposition date: 2010-10-16, release date: 2011-03-09, Last modification date: 2024-11-27) |
| Primary citation | Docquier, J.D.,Benvenuti, M.,Calderone, V.,Rossolini, G.M.,Mangani, S. Structure of the extended-spectrum [beta]-lactamase TEM-72 inhibited by citrate Acta Crystallogr.,Sect.F, 67:303-306, 2011 Cited by PubMed Abstract: TEM-72, a class A β-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum β-lactamase (ESBL) properties arising from the G238S and E240K substitutions. Although many structures of TEM variants have been published, they do not include an enzyme with the simultaneous presence of both of the ESBL-conferring G238S and E240K substitutions. Furthermore, the structure shows the presence of a citrate anion bound to the TEM-72 active site, where it interacts with all of the conserved residues of class A β-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine β-lactamases. PubMed: 21393831DOI: 10.1107/S1744309110054680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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