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Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site
- Xu, Qingping;
- Grant, Joanna;
- Chiu, Hsiu-Ju;
- Farr, Carol L;
- Jaroszewski, Lukasz;
- Knuth, Mark W;
- Miller, Mitchell D;
- Lesley, Scott A;
- Godzik, Adam;
- Elsliger, Marc-André;
- Deacon, Ashley M;
- Wilson, Ian A
Published Web Location
https://doi.org/10.1002/prot.24362Abstract
PF10014 is a novel family of 2-oxyglutarate-Fe(2+) -dependent dioxygenases that are involved in biosynthesis of antibiotics and regulation of biofilm formation, likely by catalyzing hydroxylation of free amino acids or other related ligands. The crystal structure of a PF10014 member from Methylibium petroleiphilum at 1.9 Å resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the β-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site.
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