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Proteins. 2014 Jan;82(1):164-70. doi: 10.1002/prot.24362. Epub 2013 Sep 10.

Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site.

Author information

1
Joint Center for Structural Genomics, La Jolla, California (http://www.jcsg.org); Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, 94025.

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.

KEYWORDS:

2-oxyglutarate; PF10014/BsmA; cupin dioxygenase; ferrous iron; free amino acids

PMID:
23852666
PMCID:
PMC3920835
DOI:
10.1002/prot.24362
[Indexed for MEDLINE]
Free PMC Article

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