4ID4

Crystal structure of chimeric beta-lactamase cTEM-17m

4ID4 の概要

• エントリーDOI: 10.2210/pdb4id4/pdb
• 関連するPDBエントリー: 4GPP
• 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: beta-lactamase, 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: 29077.53

構造登録者

Park, J.,Gobeil, S.,Pelletier, J.N.,Berghuis, A.M. (登録日: 2012-12-11, 公開日: 2013-12-25, 最終更新日: 2024-10-30)

主引用文献

Gobeil, S.M.,Clouthier, C.M.,Park, J.,Gagne, D.,Berghuis, A.M.,Doucet, N.,Pelletier, J.N.
Maintenance of Native-like Protein Dynamics May Not Be Required for Engineering Functional Proteins.
Chem.Biol., 21:1330-1340, 2014

PubMed Abstract: Proteins are dynamic systems, and understanding dynamics is critical for fully understanding protein function. Therefore, the question of whether laboratory engineering has an impact on protein dynamics is of general interest. Here, we demonstrate that two homologous, naturally evolved enzymes with high degrees of structural and functional conservation also exhibit conserved dynamics. Their similar set of slow timescale dynamics is highly restricted, consistent with evolutionary conservation of a functionally important feature. However, we also show that dynamics of a laboratory-engineered chimeric enzyme obtained by recombination of the two homologs exhibits striking difference on the millisecond timescale, despite function and high-resolution crystal structure (1.05 Å) being conserved. The laboratory-engineered chimera is thus functionally tolerant to modified dynamics on the timescale of catalytic turnover. Tolerance to dynamic variation implies that maintenance of native-like protein dynamics may not be required when engineering functional proteins.

PubMed: 25200606
DOI: 10.1016/j.chembiol.2014.07.016

実験手法

X-RAY DIFFRACTION (1.05 Å)