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The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

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Author(s)

Greg Mann, Jesko Alexander Johannes Gunter Koehnke, Andrew Frank Bent, Rachael Graham, Wael Houssen, Marcel Jaspars, Uli Schwarz-Linek, Jim Naismith

School/Research organisations

Abstract

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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Details

Original languageEnglish
Pages (from-to)1597-1603
Number of pages7
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
VolumeF70
Early online date14 Nov 2014
DOIs
Publication statusPublished - Dec 2014

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