5IX1

Crystal structure of mouse Morc3 ATPase-CW cassette in complex with AMPPNP and H3K4me3 peptide

5IX1 の概要

• エントリーDOI: 10.2210/pdb5ix1/pdb
• 関連するPDBエントリー: 5IX2
• 分子名称: MORC family CW-type zinc finger protein 3, Peptide from Histone H3.1, ZINC ION, ... (6 entities in total)
• 機能のキーワード: morc3, atpase, cw domain, h3k4me3, transcription
• 由来する生物種: Mus musculus (Mouse); 詳細
• 細胞内の位置: Nucleus, nucleoplasm : F7BJB9; Nucleus: P68433
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108308.53

構造登録者

Li, S.,Du, J.,Patel, D.J. (登録日: 2016-03-23, 公開日: 2016-08-17, 最終更新日: 2016-09-14)

主引用文献

Li, S.,Yen, L.,Pastor, W.A.,Johnston, J.B.,Du, J.,Shew, C.J.,Liu, W.,Ho, J.,Stender, B.,Clark, A.T.,Burlingame, A.L.,Daxinger, L.,Patel, D.J.,Jacobsen, S.E.
Mouse MORC3 is a GHKL ATPase that localizes to H3K4me3 marked chromatin
Proc.Natl.Acad.Sci.USA, 113:E5108-E5116, 2016

PubMed Abstract: Microrchidia (MORC) proteins are GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPases that function in gene regulation in multiple organisms. Animal MORCs also contain CW-type zinc finger domains, which are known to bind to modified histones. We solved the crystal structure of the murine MORC3 ATPase-CW domain bound to the nucleotide analog AMPPNP (phosphoaminophosphonic acid-adenylate ester) and in complex with a trimethylated histone H3 lysine 4 (H3K4) peptide (H3K4me3). We observed that the MORC3 N-terminal ATPase domain forms a dimer when bound to AMPPNP. We used native mass spectrometry to show that dimerization is ATP-dependent, and that dimer formation is enhanced in the presence of nonhydrolyzable ATP analogs. The CW domain uses an aromatic cage to bind trimethylated Lys4 and forms extensive hydrogen bonds with the H3 tail. We found that MORC3 localizes to promoters marked by H3K4me3 throughout the genome, consistent with its binding to H3K4me3 in vitro. Our work sheds light on aspects of the molecular dynamics and function of MORC3.

PubMed: 27528681
DOI: 10.1073/pnas.1609709113

実験手法

X-RAY DIFFRACTION (2.6 Å)