2O6V

Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

2O6V の概要

• エントリーDOI: 10.2210/pdb2o6v/pdb
• 分子名称: Ubiquitin, SULFATE ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (6 entities in total)
• 機能のキーワード: ubiquitin, tetraubiquitin, polyubiquitin, lys48-linked, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 69591.52

構造登録者

Eddins, M.J.,Wolberger, C. (登録日: 2006-12-08, 公開日: 2007-02-13, 最終更新日: 2024-11-13)

主引用文献

Eddins, M.J.,Varadan, R.,Fushman, D.,Pickart, C.M.,Wolberger, C.
Crystal Structure and Solution NMR Studies of Lys48-linked Tetraubiquitin at Neutral pH
J.Mol.Biol., 367:204-211, 2007

PubMed Abstract: Ubiquitin modification of proteins is used as a signal in many cellular processes. Lysine side-chains can be modified by a single ubiquitin or by a polyubiquitin chain, which is defined by an isopeptide bond between the C terminus of one ubiquitin and a specific lysine in a neighboring ubiquitin. Polyubiquitin conformations that result from different lysine linkages presumably differentiate their roles and ability to bind specific targets and enzymes. However, conflicting results have been obtained regarding the precise conformation of Lys48-linked tetraubiquitin. We report the crystal structure of Lys48-linked tetraubiquitin at near-neutral pH. The two tetraubiquitin complexes in the asymmetric unit show the complete connectivity of the chain and the molecular details of the interactions. This tetraubiquitin conformation is consistent with our NMR data as well as with previous studies of diubiquitin and tetraubiquitin in solution at neutral pH. The structure provides a basis for understanding Lys48-linked polyubiquitin recognition under physiological conditions.

PubMed: 17240395
DOI: 10.1016/j.jmb.2006.12.065

実験手法

X-RAY DIFFRACTION (2.2 Å)