5YZV

Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA

5YZV の概要

• エントリーDOI: 10.2210/pdb5yzv/pdb
• 分子名称: Probable serine/threonine-protein kinase PkwA (2 entities in total)
• 機能のキーワード: prokaryotic, thermostable, reversible folding, protein binding
• 由来する生物種: Thermomonospora curvata
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 159984.27

構造登録者

Li, D.Y.,Shen, C.,Du, Y.,Qiao, F.F.,Kong, T.,Yuan, L.R.,Zhang, D.L.,Wu, X.H.,Wu, Y.D. (登録日: 2017-12-15, 公開日: 2018-10-03, 最終更新日: 2024-03-27)

主引用文献

Shen, C.,Du, Y.,Qiao, F.,Kong, T.,Yuan, L.,Zhang, D.,Wu, X.,Li, D.,Wu, Y.D.
Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA
Sci Rep, 8:12965-12965, 2018

PubMed Abstract: WD40 proteins belong to a big protein family with members identified in every eukaryotic proteome. However, WD40 proteins were only reported in a few prokaryotic proteomes. Using WDSP ( http://wu.scbb.pkusz.edu.cn/wdsp/ ), a prediction tool, we identified thousands of prokaryotic WD40 proteins, among which few proteins have been biochemically characterized. As shown in our previous bioinformatics study, a large proportion of prokaryotic WD40 proteins have higher intramolecular sequence identity among repeats and more hydrogen networks, which may indicate better stability than eukaryotic WD40s. Here we report our biophysical and structural study on the WD40 domain of PkwA from Thermomonospora curvata (referred as tPkwA-C). We demonstrated that the stability of thermophilic tPkwA-C correlated to ionic strength and tPkwA-C exhibited fully reversible unfolding under different denaturing conditions. Therefore, the folding kinetics was also studied through stopped-flow circular dichroism spectra. The crystal structure of tPkwA-C was further resolved and shed light on the key factors that stabilize its beta-propeller structure. Like other WD40 proteins, DHSW tetrad has a significant impact on the stability of tPkwA-C. Considering its unique features, we proposed that tPkwA-C should be a great structural template for protein engineering to study key residues involved in protein-protein interaction of a WD40 protein.

PubMed: 30154510
DOI: 10.1038/s41598-018-31140-y

実験手法

X-RAY DIFFRACTION (2.6 Å)