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The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster
Author(s) -
Mann Greg,
Koehnke Jesko,
Bent Andrew F.,
Graham Rachael,
Houssen Wael,
Jaspars Marcel,
SchwarzLinek Uli,
Naismith James H.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x1402425x
Subject(s) - biosynthesis , gene cluster , function (biology) , domain (mathematical analysis) , computational biology , gene , sequence (biology) , protein domain , biology , architecture domain , protein structure , stereochemistry , chemistry , biochemistry , genetics , computer science , mathematical analysis , mathematics , software architecture , software , enterprise architecture framework , programming language
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.