Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site
Year: 2013
Type: article
Abstract: 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.
DOI: 10.1002/prot.24362
Institutions: SLAC National Accelerator Laboratory, Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, Genomics Institute of the Novartis Research Foundation, Scripps Research Institute, Sanford Burnham Prebys Medical Discovery Institute, University of California San Diego
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W2124064258