4R4R

Crystal structure of chimeric beta-lactamase cTEM-19m at 1.2 angstrom resolution

4R4R の概要

• エントリーDOI: 10.2210/pdb4r4r/pdb
• 関連するPDBエントリー: 4ID4 4MEZ
• 分子名称: Beta-lactamase TEM,Beta-lactamase PSE-4, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29042.56

構造登録者

Park, J.,Gobeil, S.,Pelletier, J.N.,Berghuis, A.M. (登録日: 2014-08-19, 公開日: 2015-11-11, 最終更新日: 2024-10-16)

主引用文献

Gobeil, S.M.C.,Ebert, M.C.C.J.C.,Park, J.,Gagne, D.,Doucet, N.,Berghuis, A.M.,Pleiss, J.,Pelletier, J.N.
The Structural Dynamics of Engineered beta-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function.
Sci Rep, 9:6656-6656, 2019

PubMed Abstract: Understanding the principles of protein dynamics will help guide engineering of protein function: altering protein motions may be a barrier to success or may be an enabling tool for protein engineering. The impact of dynamics on protein function is typically reported over a fraction of the full scope of motional timescales. If motional patterns vary significantly at different timescales, then only by monitoring motions broadly will we understand the impact of protein dynamics on engineering functional proteins. Using an integrative approach combining experimental and in silico methodologies, we elucidate protein dynamics over the entire span of fast to slow timescales (ps to ms) for a laboratory-engineered system composed of five interrelated β-lactamases: two natural homologs and three laboratory-recombined variants. Fast (ps-ns) and intermediate (ns-µs) dynamics were mostly conserved. However, slow motions (µs-ms) were few and conserved in the natural homologs yet were numerous and widely dispersed in their recombinants. Nonetheless, modified slow dynamics were functionally tolerated. Crystallographic B-factors from high-resolution X-ray structures were partly predictive of the conserved motions but not of the new slow motions captured in our solution studies. Our inspection of protein dynamics over a continuous range of timescales vividly illustrates the complexity of dynamic impacts of protein engineering as well as the functional tolerance of an engineered enzyme system to new slow motions.

PubMed: 31040324
DOI: 10.1038/s41598-019-42866-8

実験手法

X-RAY DIFFRACTION (1.2 Å)