6F4S

Human JMJD5 (N308C) in complex with Mn(II), 2OG and RCCD1 (139-143) (complex-4)

6F4S の概要

• エントリーDOI: 10.2210/pdb6f4s/pdb
• 関連するPDBエントリー: 6F4M 6F4N 6F4O 6F4P 6F4Q 6F4R 6F4T
• 分子名称: JmjC domain-containing protein 5, RCC1 domain-containing protein 1, MANGANESE (II) ION, ... (7 entities in total)
• 機能のキーワード: oxidoreductase, non-heme, iron, 2-oxoglutarate, dioxygenase, jmjc, jmjc domain, lysine-specific demethylase 8, jmjc domain-containing protein 5, arginyl c-3 hydroxylase, jmjd5, kdm8, oxygenase, hypoxia, dna-binding, metal-binding, translation, dsbh, facial triad, cytoplasm, jmjc hydroxylase, jmjc demethylase, kdms, post-translational modifications, ptm, beta-hydroxylation, hydroxylation, arginine hydroxylation, rcc1 domain-containing protein 1, rccd1, regulator of chromosome condensation, 40s ribosomal protein s6, rps6, ribosome biogenesis, transcription, epigenetic regulation, signaling, development, cell structure, transcription activator/inhibitor, phosphorylation, cancer, polymorphism
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q8N371; Chromosome : A6NED2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30526.22

構造登録者

Chowdhury, R.,Islam, M.S.,Schofield, C.J. (登録日: 2017-11-30, 公開日: 2018-04-04, 最終更新日: 2024-10-23)

主引用文献

Wilkins, S.E.,Islam, S.,Gannon, J.M.,Markolovic, S.,Hopkinson, R.J.,Ge, W.,Schofield, C.J.,Chowdhury, R.
JMJD5 is a human arginyl C-3 hydroxylase.
Nat Commun, 9:1180-1180, 2018

PubMed Abstract: Oxygenase-catalysed post-translational modifications of basic protein residues, including lysyl hydroxylations and N-methyl lysyl demethylations, have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone N-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6). High-resolution crystallographic analyses reveal overall fold, active site and substrate binding/product release features supporting the assignment of JMJD5 as an arginine hydroxylase rather than a KDM. The results will be useful in the development of selective oxygenase inhibitors for the treatment of cancer and genetic diseases.

PubMed: 29563586
DOI: 10.1038/s41467-018-03410-w

実験手法

X-RAY DIFFRACTION (1.461 Å)