Structural basis for the interaction of lactivicins with serine beta-lactamases.
Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV a...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797077073168171008 |
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| author | Brown, T Charlier, P Herman, R Schofield, C Sauvage, E |
| author_facet | Brown, T Charlier, P Herman, R Schofield, C Sauvage, E |
| author_sort | Brown, T |
| collection | OXFORD |
| description | Lactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics. |
| first_indexed | 2024-03-07T00:12:35Z |
| format | Journal article |
| id | oxford-uuid:79be0f9e-2abc-472d-a3d1-88207e790fb1 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:12:35Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:79be0f9e-2abc-472d-a3d1-88207e790fb12022-03-26T20:39:20ZStructural basis for the interaction of lactivicins with serine beta-lactamases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:79be0f9e-2abc-472d-a3d1-88207e790fb1EnglishSymplectic Elements at Oxford2010Brown, TCharlier, PHerman, RSchofield, CSauvage, ELactivicin (LTV) is a natural non-beta-lactam antibiotic that inhibits penicillin-binding proteins and serine beta-lactamases. A crystal structure of a BS3-LTV complex reveals that, as for its reaction with PBPs, LTV reacts with the nucleophilic serine and that cycloserine and lactone rings of LTV are opened. This structure, together with reported structures of PBP1b with lactivicins, provides a basis for developing improved lactivicin-based gamma-lactam antibiotics. |
| spellingShingle | Brown, T Charlier, P Herman, R Schofield, C Sauvage, E Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title | Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title_full | Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title_fullStr | Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title_full_unstemmed | Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title_short | Structural basis for the interaction of lactivicins with serine beta-lactamases. |
| title_sort | structural basis for the interaction of lactivicins with serine beta lactamases |
| work_keys_str_mv | AT brownt structuralbasisfortheinteractionoflactivicinswithserinebetalactamases AT charlierp structuralbasisfortheinteractionoflactivicinswithserinebetalactamases AT hermanr structuralbasisfortheinteractionoflactivicinswithserinebetalactamases AT schofieldc structuralbasisfortheinteractionoflactivicinswithserinebetalactamases AT sauvagee structuralbasisfortheinteractionoflactivicinswithserinebetalactamases |