5JGR

Spin-Labeled T4 Lysozyme Construct K43V1

5JGR の概要

• エントリーDOI: 10.2210/pdb5jgr/pdb
• 関連するPDBエントリー: 5JGN 5JGU 5JGV 5JGX 5JGZ
• 分子名称: Endolysin, S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-imidazol-4-yl) methanesulfonothioate, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: spin label, epr, deer, hydrolase
• 由来する生物種: Enterobacteria phage T4 sensu lato
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19212.27

構造登録者

Balo, A.R.,Feyrer, H.,Ernst, O.P. (登録日: 2016-04-20, 公開日: 2017-02-15, 最終更新日: 2024-10-23)

主引用文献

Balo, A.R.,Feyrer, H.,Ernst, O.P.
Toward Precise Interpretation of DEER-Based Distance Distributions: Insights from Structural Characterization of V1 Spin-Labeled Side Chains.
Biochemistry, 55:5256-5263, 2016

PubMed Abstract: Pulsed electron paramagnetic resonance experiments can measure individual distances between two spin-labeled side chains in proteins in the range of ∼1.5-8 nm. However, the flexibility of traditional spin-labeled side chains leads to diffuse spin density loci and thus distance distributions with relatively broad peaks, thereby complicating the interpretation of protein conformational states. Here we analyzed the spin-labeled V1 side chain, which is internally anchored and hence less flexible. Crystal structures of V1-labeled T4 lysozyme constructs carrying the V1 side chain on α-helical segments suggest that V1 side chains adopt only a few discrete rotamers. In most cases, only one rotamer is observed at a given site, explaining the frequently observed narrow distance distribution for doubly V1-labeled proteins. We used the present data to derive guidelines that may allow distance interpretation of other V1-labeled proteins for higher-precision structural modeling.

PubMed: 27532325
DOI: 10.1021/acs.biochem.6b00608

実験手法

X-RAY DIFFRACTION (1.46 Å)