2HB9: Crystal Structure Of The Zinc-beta-lactamase L1 From Stenotrophomonas Maltophilia (inhibitor 3)

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.
PDB ID: 2HB9Download
MMDB ID: 46196
PDB Deposition Date: 2006/6/14
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Similar Structures:
Biological Unit for 2HB9: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 2HB9
Label Count Molecule
Proteins (4 molecules)
Metallo-beta-lactamase L1
Molecule annotation
Chemicals (24 molecules)
* Click molecule labels to explore molecular sequence information.

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