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Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site
Author(s) -
Xu Qingping,
Grant Joanna,
Chiu HsiuJu,
Farr Carol L.,
Jaroszewski Lukasz,
Knuth Mark W.,
Miller Mitchell D.,
Lesley Scott A.,
Godzik Adam,
Elsliger MarcAndré,
Deacon Ashley M.,
Wilson Ian A.
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24362
Subject(s) - crystal structure , active site , fold (higher order function) , family member , stereochemistry , chemistry , biology , crystallography , biochemistry , medicine , enzyme , computer science , family medicine , programming language
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. Proteins 2014; 82:164–170. © 2013 Wiley Periodicals, Inc.