2WG6

Proteasome-Activating Nucleotidase (PAN) N-domain (57-134) from Archaeoglobus fulgidus fused to GCN4, P61A Mutant

2WG6 の概要

• エントリーDOI: 10.2210/pdb2wg6/pdb
• 関連するPDBエントリー: 1CE9 1DGC 1GCL 1GCM 1GZL 1IHQ 1IJ0 1IJ1 1IJ2 1IJ3 1KQL 1LD4 1LLM 1NKN 1PIQ 1RB1 1RB4 1RB5 1RB6 1SWI 1TMZ 1UNT 1UNU 1UNV 1UNW 1UNX 1UNY 1UNZ 1UO0 1UO1 1UO2 1UO3 1UO4 1UO5 1W5G 1W5H 1W5I 1W5J 1W5K 1W5L 1YSA 1ZII 1ZIJ 1ZIK 1ZIL 1ZIM 1ZTA 2B1F 2B22 2BNI 2CCE 2CCF 2CCN 2D3E 2DGC 2WG5 2ZTA
• 分子名称: GENERAL CONTROL PROTEIN GCN4, PROTEASOME-ACTIVATING NUCLEOTIDASE (2 entities in total)
• 機能のキーワード: transcription, hydrolase, transcription hydrolase complex, nucleotide-binding, substrate recognition, aaa protein, chaperone activity, atpase, ob fold, proteasome, atp-binding amino-acid biosynthesis, transcription regulation, nucleus, dna-binding, activator, phosphoprotein
• 由来する生物種: SACCHAROMYCES CEREVISIAE; 詳細
• 細胞内の位置: Cytoplasm : O28303
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 148609.03

構造登録者

Hartmann, M.D.,Djuranovic, S.,Ursinus, A.,Zeth, K.,Lupas, A.N. (登録日: 2009-04-15, 公開日: 2009-04-28, 最終更新日: 2023-12-13)

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 (2.5 Å)