7YXL
Drosophila melanogaster JMJD7 (dmJMJD7) in complex with Mn and N-oxalyl-D-phenylalanine (NOFD)
Summary for 7YXL
| Entry DOI | 10.2210/pdb7yxl/pdb |
| Descriptor | GH14974p, MANGANESE (II) ION, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | oxidoreductase, non-heme, iron, 2-oxoglutarate, dioxygenase, oxygenase, jmjc, jmjc domain, jmjc domain-containing protein 7, jmjd7, jmjc hydroxylase, jmjc demethylase, kdms, post-translational modifications, ptm, hydroxylation, lysyl hydroxylation, dimerisation, translation factor, developmentally regulated gtp binding proteins, drg1, drg2, trafac gtpase, hypoxia, nucleic acid- binding, metal-binding, translation, helix-loop-helix-beta, dsbh, facial triad, development, cancer, ribosome biogenesis |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 74614.09 |
| Authors | Chowdhury, R.,Schofield, C.J. (deposition date: 2022-02-16, release date: 2022-04-27, Last modification date: 2024-10-23) |
| Primary citation | Chowdhury, R.,Abboud, M.I.,Wiley, J.,Tumber, A.,Markolovic, S.,Schofield, C.J. Conservation of the unusual dimeric JmjC fold of JMJD7 from Drosophila melanogaster to humans. Sci Rep, 12:6065-6065, 2022 Cited by PubMed Abstract: 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. PubMed: 35410347DOI: 10.1038/s41598-022-10028-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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