3CM6

Crystal structure of cell-death related nuclease 4 (CRN-4) bound with Er

3CM6 の概要

• エントリーDOI: 10.2210/pdb3cm6/pdb
• 関連するPDBエントリー: 3CG7 3CM5
• 分子名称: Cell death-related nuclease 4, ZINC ION, ERBIUM (III) ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, apoptosis, apoptotic nuclease, 3'-5' exonuclease, dedd family
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71650.59

構造登録者

Hsiao, Y.-Y.,Yuan, H.S. (登録日: 2008-03-21, 公開日: 2008-12-30, 最終更新日: 2023-11-01)

主引用文献

Hsiao, Y.-Y.,Nakagawa, A.,Shi, Z.,Mitani, S.,Xue, D.,Yuan, H.S.
Crystal structure of CRN-4: implications for domain function in apoptotic DNA degradation
Mol.Cell.Biol., 29:448-457, 2009

PubMed Abstract: Cell death related nuclease 4 (CRN-4) is one of the apoptotic nucleases involved in DNA degradation in Caenorhabditis elegans. To understand how CRN-4 is involved in apoptotic DNA fragmentation, we analyzed CRN-4's biochemical properties, in vivo cell functions, and the crystal structures of CRN-4 in apo-form, Mn(2+)-bound active form, and Er(3+)-bound inactive form. CRN-4 is a dimeric nuclease with the optimal enzyme activity in cleaving double-stranded DNA in apoptotic salt conditions. Both mutational studies and the structures of the Mn(2+)-bound CRN-4 revealed the geometry of the functional nuclease active site in the N-terminal DEDDh domain. The C-terminal domain, termed the Zn-domain, contains basic surface residues ideal for nucleic acid recognition and is involved in DNA binding, as confirmed by deletion assays. Cell death analysis in C. elegans further demonstrated that both the nuclease active site and the Zn-domain are required for crn-4's function in apoptosis. Combining all of the data, we suggest a structural model where chromosomal DNA is bound at the Zn-domain and cleaved at the DEDDh nuclease domain in CRN-4 when the cell is undergoing apoptosis.

PubMed: 18981218
DOI: 10.1128/MCB.01006-08

実験手法

X-RAY DIFFRACTION (2.6 Å)