Langan, P.S. and Vandavasi, V.G. and Weiss, K. and Cooper, Jonathan B. and Ginell, S.L. and Coates, L. (2016) The structure of Toho1 β-lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition. FEBS Open Bio 6 (12), pp. 1170-1177. ISSN 2211-5463.
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Abstract
The role of the conserved residue Tyr105 in class A β-lactamases has been the subject of investigation using both structural studies and saturation mutagenesis. Both have shown that while it does not need to be strictly conserved for activity, it is important for substrate recognition. With this in mind we determined the crystal structure of Toho1 β-lactamase at 15 K to 1.10 Å resolution in complex with penicillin. As expected a ring-opened penicillin molecule bound to Ser70 the catalytic nucleophile, can clearly be seen in electron density in the active site. In addition to the trapped penicillin, however, are two additional intact ring-closed penicillin molecules, captured by the enzyme through noncovalent interactions at the edge of the active site.
Metadata
| Item Type: | Article |
|---|---|
| Keyword(s) / Subject(s): | antibiotic resistance, antibiotics, enzyme, enzyme structure, X-ray crystallography |
| School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
| Depositing User: | Administrator |
| Date Deposited: | 07 Mar 2017 16:46 |
| Last Modified: | 02 Aug 2023 17:30 |
| URI: | https://eprints.bbk.ac.uk/id/eprint/17770 |
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