6CDD

Npl4 zinc finger and MPN domains (Chaetomium thermophilum)

6CDD の概要

• エントリーDOI: 10.2210/pdb6cdd/pdb
• 分子名称: Npl4 zinc finger, ZINC ION (3 entities in total)
• 機能のキーワード: aaa atpase cofactor, zinc finger, mpn, protein binding
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107493.08

構造登録者

Bodnar, N.O.,Rapoport, T.A. (登録日: 2018-02-08, 公開日: 2018-07-04, 最終更新日: 2024-04-03)

主引用文献

Bodnar, N.O.,Kim, K.H.,Ji, Z.,Wales, T.E.,Svetlov, V.,Nudler, E.,Engen, J.R.,Walz, T.,Rapoport, T.A.
Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4.
Nat. Struct. Mol. Biol., 25:616-622, 2018

PubMed Abstract: Many polyubiquitinated proteins are extracted from membranes or complexes by the conserved ATPase Cdc48 (in yeast; p97 or VCP in mammals) before proteasomal degradation. Each Cdc48 hexamer contains two stacked ATPase rings (D1 and D2) and six N-terminal (N) domains. Cdc48 binds various cofactors, including the Ufd1-Npl4 heterodimer. Here, we report structures of the Cdc48-Ufd1-Npl4 complex from Chaetomium thermophilum. Npl4 interacts through its UBX-like domain with a Cdc48 N domain, and it uses two Zn-finger domains to anchor the enzymatically inactive Mpr1-Pad1 N-terminal (MPN) domain, homologous to domains found in several isopeptidases, to the top of the D1 ATPase ring. The MPN domain of Npl4 is located above Cdc48's central pore, a position similar to the MPN domain from deubiquitinase Rpn11 in the proteasome. Our results indicate that Npl4 is unique among Cdc48 cofactors and suggest a mechanism for binding and translocation of polyubiquitinated substrates into the ATPase.

PubMed: 29967539
DOI: 10.1038/s41594-018-0085-x

実験手法

X-RAY DIFFRACTION (2.58233712092 Å)