2L83

A protein from Haloferax volcanii

2L83 の概要

• エントリーDOI: 10.2210/pdb2l83/pdb
• NMR情報: BMRB: 17391
• 分子名称: Small archaeal modifier protein 1 (1 entity in total)
• 機能のキーワード: protein binding
• 由来する生物種: Haloferax volcanii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10014.93

構造登録者

Zhang, W.,Liao, S.,Fan, K.,Tu, X. (登録日: 2011-01-03, 公開日: 2012-01-11, 最終更新日: 2024-05-15)

主引用文献

Ye, K.,Liao, S.,Zhang, W.,Fan, K.,Zhang, X.,Zhang, J.,Xu, C.,Tu, X.
Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.
Protein Sci., 22:1174-1182, 2013

PubMed Abstract: Eukaryotic ubiquitin and ubiquitin-like systems play crucial roles in various cellular biological processes. In this work, we determined the solution structure of SAMP1 from Haloferax volcanii by NMR spectroscopy. Under low ionic conditions, SAMP1 presented two distinct conformations, one folded β-grasp and the other disordered. Interestingly, SAMP1 underwent a conformational conversion from disorder to order with ion concentration increasing, indicating that the ordered conformation is the functional form of SAMP1 under the physiological condition of H. volcanii. Furthermore, SAMP1 could interact with proteasome-activating nucleotidase B, supposing a potential role of SAMP1 in the protein degradation pathway mediated by proteasome.

PubMed: 23818097
DOI: 10.1002/pro.2302

実験手法

SOLUTION NMR