Gurel, Guliz;
Blaha, Gregor;
Steitz, Thomas A;
Moore, Peter B;
(2009)
Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui.
Antimicrobial Agents and Chemotherapy
, 53
(12)
pp. 5010-5014.
10.1128/AAC.00817-09.
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Abstract
Structures have been obtained for the complexes that triacetyloleandomycin and mycalamide A form with the large ribosomal subunit of Haloarcula marismortui. Triacetyloleandomycin binds in the nascent peptide tunnel and inhibits the activity of ribosomes by blocking the growth of the nascent peptide chain. Mycalamide A binds to the E site and inhibits protein synthesis by occupying the space normally occupied by the CCA end of E-site-bound tRNAs.
| Type: | Article |
|---|---|
| Title: | Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui |
| Location: | United States |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1128/AAC.00817-09 |
| Publisher version: | http://dx.doi.org/10.1128/aac.00817-09 |
| Language: | English |
| Additional information: | This version is the version of record. For information on re-use, please refer to the publisher’s terms and conditions. |
| Keywords: | Science & Technology, Life Sciences & Biomedicine, Microbiology, Pharmacology & Pharmacy, PEPTIDYL-TRANSFERASE CENTER, TRANSFER-RNA, BOND FORMATION, E-SITE, ANTIBIOTICS, MECHANISM, MACROLIDE, 13-DEOXYTEDANOLIDE, RESOLUTION, RESISTANT |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Cell and Developmental Biology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10186851 |
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