1TR8

Crystal Structure of archaeal Nascent Polypeptide-associated Complex (aeNAC)

1TR8 の概要

• エントリーDOI: 10.2210/pdb1tr8/pdb
• 分子名称: conserved protein (MTH177) (2 entities in total)
• 機能のキーワード: chaperones, nascent polypeptide-associated complex, ribosome, uba-domain, ubiquitin, chaperone
• 由来する生物種: Methanothermobacter marburgensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23928.80

構造登録者

Spreter, T.,Pech, M.,Beatrix, B. (登録日: 2004-06-21, 公開日: 2005-02-01, 最終更新日: 2024-11-20)

主引用文献

Spreter, T.,Pech, M.,Beatrix, B.
The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a UBA domain
J.Biol.Chem., 280:15849-15854, 2005

PubMed Abstract: Nascent polypeptide-associated complex (NAC) was identified in eukaryotes as the first cytosolic factor that contacts the nascent polypeptide chain emerging from the ribosome. NAC is highly conserved from yeast to humans. Mutations in NAC cause severe embryonically lethal phenotypes in mice, Drosophila, and Caenorhabditis elegans. NAC was suggested to protect the nascent chain from inappropriate early interactions with cytosolic factors. Eukaryotic NAC is a heterodimer with two subunits sharing substantial homology with each other. All sequenced archaebacterial genomes exhibit only one gene homologous to the NAC subunits. Here we present the first archaebacterial NAC homolog. It forms a homodimer, and as eukaryotic NAC it is associated with ribosomes and contacts the emerging nascent chain on the ribosome. We present the first crystal structure of a NAC protein revealing two structural features: (i) a novel unique protein fold that mediates dimerization of the complex, and (ii) a ubiquitin-associated domain that suggests a yet unidentified role for NAC in the cellular protein quality control system via the ubiquitination pathway. Based on the presented structure we propose a model for the eukaryotic heterodimeric NAC domain.

PubMed: 15665334
DOI: 10.1074/jbc.M500160200

実験手法

X-RAY DIFFRACTION (2.27 Å)