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


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.

SUBMITTER: Mann G 

PROVIDER: S-EPMC4259220 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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

Mann Greg G   Koehnke Jesko J   Bent Andrew F AF   Graham Rachael R   Houssen Wael W   Jaspars Marcel M   Schwarz-Linek Uli U   Naismith James H JH  

Acta crystallographica. Section F, Structural biology communications 20141114 Pt 12


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 charact  ...[more]

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