Structural highlights
Publication Abstract from PubMed
The JmjC family of 2-oxoglutarate dependent oxygenases catalyse a range of hydroxylation and demethylation reactions in humans and other animals. Jumonji domain-containing 7 (JMJD7) is a JmjC (3S)-lysyl-hydroxylase that catalyses the modification of Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1 and 2); JMJD7 has also been reported to have histone endopeptidase activity. Here we report biophysical and biochemical studies on JMJD7 from Drosophila melanogaster (dmJMJD7). Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7). The results further support the assignment of JMJD7 as a lysyl hydroxylase and will help enable the development of selective inhibitors for it and other JmjC oxygenases.
Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans.,Chowdhury R, Abboud MI, Wiley J, Tumber A, Markolovic S, Schofield CJ Sci Rep. 2022 Apr 11;12(1):6065. doi: 10.1038/s41598-022-10028-y. PMID:35410347[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chowdhury R, Abboud MI, Wiley J, Tumber A, Markolovic S, Schofield CJ. Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans. Sci Rep. 2022 Apr 11;12(1):6065. doi: 10.1038/s41598-022-10028-y. PMID:35410347 doi:https://dx.doi.org/10.1038/s41598-022-10028-y
