2FU7

Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (Cu-substituted form)

Summary for 2FU7

• Entry DOI: 10.2210/pdb2fu7/pdb
• Related: 2FM6 2FU6 2FU8 2FU9
• Descriptor: Metallo-beta-lactamase L1, COPPER (II) ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, zn, metallo, beta, lactamase
• Biological source: Stenotrophomonas maltophilia
• Cellular location: Periplasm (Potential): P52700
• Total number of polymer chains: 2
• Total formula weight: 58983.16

Authors

Nauton, L.,Garau, G.,Kahn, R.,Dideberg, O. (deposition date: 2006-01-26, release date: 2007-01-30, Last modification date: 2024-10-23)

Primary citation

Nauton, L.,Kahn, R.,Garau, G.,Hernandez, J.F.,Dideberg, O.
Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
J.Mol.Biol., 375:257-269, 2008

PubMed Abstract: One mechanism by which bacteria can escape the action of beta-lactam antibiotics is the production of metallo-beta-lactamases. Inhibition of these enzymes should restore the action of these widely used antibiotics. The tetrameric enzyme L1 from Stenotrophomonas maltophilia was used as a model system to determine a series of high-resolution crystal structures of apo, mono and bi-metal substituted proteins as well as protein-inhibitor complexes. Unexpectedly, although the apo structure revealed only few significant structural differences from the holo structure, some inhibitors were shown to induce amino acid side-chain rotations in the tightly packed active site. Moreover, one inhibitor employs a new binding mode in order to interact with the di-zinc center. This structural information could prove essential in the process of elucidation of the mode of interaction between a putative lead compound and metallo-beta-lactamases, one of the main steps in structure-based drug design.

PubMed: 17999929
DOI: 10.1016/j.jmb.2007.10.036

Experimental method

X-RAY DIFFRACTION (1.85 Å)