Structural highlights
Function
A2SJH7_METPP
Publication Abstract from PubMed
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 A resolution shows strong structural similarity to cupin dioxygenases in overall fold and active site, despite very remote homology. However, one of the beta-strands of the cupin catalytic core is replaced by a loop that displays conformational isomerism that likely regulates the active site.
Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site.,Xu Q, Grant J, Chiu HJ, Farr CL, Jaroszewski L, Knuth MW, Miller MD, Lesley SA, Godzik A, Elsliger MA, Deacon AM, Wilson IA Proteins. 2014 Jan;82(1):164-70. doi: 10.1002/prot.24362. Epub 2013 Sep 10. PMID:23852666[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu Q, Grant J, Chiu HJ, Farr CL, Jaroszewski L, Knuth MW, Miller MD, Lesley SA, Godzik A, Elsliger MA, Deacon AM, Wilson IA. Crystal structure of a member of a novel family of dioxygenases (PF10014) reveals a conserved cupin fold and active site. Proteins. 2014 Jan;82(1):164-70. doi: 10.1002/prot.24362. Epub 2013 Sep 10. PMID:23852666 doi:http://dx.doi.org/10.1002/prot.24362