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| {{STRUCTURE_2hb9| PDB=2hb9 | SCENE= }} | | {{STRUCTURE_2hb9| PDB=2hb9 | SCENE= }} |
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| '''Crystal Structure of the Zinc-Beta-Lactamase L1 from Stenotrophomonas Maltophilia (Inhibitor 3)'''
| | ===Crystal Structure of the Zinc-Beta-Lactamase L1 from Stenotrophomonas Maltophilia (Inhibitor 3)=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17999929}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17999929 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17999929}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Metallo]] | | [[Category: Metallo]] |
| [[Category: Zn]] | | [[Category: Zn]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:15:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:25:47 2008'' |
