期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 70, 期 -, 页码 1597-1603出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X1402425X
关键词
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资金
- BBSRC [BB/K015508/1]
- ERC (TNT-LEAP)
- Wellcome Trust Capital Award [086036]
- SULSA Leaders award
- BBSRC [BB/K015508/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [1098674, BB/K015508/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1245361] Funding Source: researchfish
Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.
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