The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster
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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.
Mann , G , Koehnke , J A J G , Bent , A F , Graham , R , Houssen , W , Jaspars , M , Schwarz-Linek , U & Naismith , J 2014 , ' The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster ' Acta Crystallographica. Section F, Structural biology and crystallization communications , vol F70 , pp. 1597-1603 . DOI: 10.1107/S2053230X1402425X
Acta Crystallographica. Section F, Structural biology and crystallization communications
©2014. The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
DescriptionThis work was funded by the BBSRC (BB/K015508/1) and ERC (TNT-LEAP), and the University of St Andrews infrastructure is supported by a Wellcome Trust Capital Award (086036). WH is the recipient of the SULSA Leaders award.
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