2WFW

Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure

2WFW の概要

• エントリーDOI: 10.2210/pdb2wfw/pdb
• 分子名称: ARC (2 entities in total)
• 機能のキーワード: atp-binding protein, proteasomal atpases, pan, arc, aaa, atp-binding, nucleotide-binding
• 由来する生物種: RHODOCOCCUS ERYTHROPOLIS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 49823.02

構造登録者

Djuranovic, S.,Hartmann, M.D.,Habeck, M.,Ursinus, A.,Zwickl, P.,Martin, J.,Lupas, A.N.,Zeth, K. (登録日: 2009-04-15, 公開日: 2009-05-12, 最終更新日: 2024-05-08)

主引用文献

Djuranovic, S.,Hartmann, M.D.,Habeck, M.,Ursinus, A.,Zwickl, P.,Martin, J.,Lupas, A.N.,Zeth, K.
Structure and Activity of the N-Terminal Substrate Recognition Domains in Proteasomal Atpases.
Mol.Cell, 34:580-, 2009

PubMed Abstract: The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings.

PubMed: 19481487
DOI: 10.1016/J.MOLCEL.2009.04.030

実験手法

X-RAY DIFFRACTION (1.6 Å)