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
Joint Center for Structural Genomics, La Jolla, California (http://www.jcsg.org); Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California, 94025.
Proteins. 2014 Jan;82(1):164-70. doi: 10.1002/prot.24362. Epub 2013 Sep 10.
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.
PF10014是一类新型的依赖2-氧代戊二酸-Fe(2+)的双加氧酶，参与抗生素的生物合成和生物膜形成的调控，可能是通过催化游离氨基酸或其他相关配体的羟基化来实现的。来自嗜油甲基杆菌的PF10014成员在1.9 Å分辨率下的晶体结构显示，尽管同源性非常远，但在整体折叠和活性位点上与铜蛋白双加氧酶具有很强的结构相似性。然而，铜蛋白催化核心的一条β链被一个环取代，该环表现出构象异构现象，可能对活性位点进行调控。
