期刊
MOLECULAR CELL
卷 73, 期 4, 页码 749-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2018.11.032
关键词
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资金
- RFBR-Royal Society International Exchanges Scheme [KO165410043/IE160246]
- Skoltech
- National Science Centre, Poland [UMO-2015/19/P/NZ1/03137]
- European Union [665778]
- Biotechnology and Biosciences Research Council (UK) Institute Strategic Programme [BB/J004561/1, BB/P012523/1]
- NIH [RO1 AI117210]
- European Community [283570]
- BBSRC [BBS/E/J/000PR9791] Funding Source: UKRI
The introduction of azole heterocycles into a peptide backbone is the principal step in the biosynthesis of numerous compounds with therapeutic potential. One of them is microcin B17, a bacterial topoisomerase inhibitor whose activity depends on the conversion of selected serine and cysteine residues of the precursor peptide to oxazoles and thiazoles by the McbBCD synthetase complex. Crystal structures of McbBCD reveal an octameric B4C2D2 complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer. An atomic-level view of the azole synthetase is a starting point for deeper understanding and control of biosynthesis of a large group of ribosomally synthesized natural products.
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