BIROn - Birkbeck Institutional Research Online

    The structure of Toho1 β-lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition

    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.

    [img]
    Preview
    Text
    17770.pdf - Published Version of Record
    Available under License Creative Commons Attribution.

    Download (1MB) | Preview

    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 Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 07 Mar 2017 16:46
    Last Modified: 27 Jul 2019 05:33
    URI: http://eprints.bbk.ac.uk/id/eprint/17770

    Statistics

    Downloads
    Activity Overview
    116Downloads
    89Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item