Structural and molecular dynamic studies of Pseudomonas aeruginosa OdaA reveal the regulation role of a C-terminal hinge element

• Published in: Biochimica et biophysica acta. General subjects Vol. 1865; no. 1; p. 129756
• Main Authors: Zhao, Ning-lin, Zhang, Qian-qian, Zhao, Chang, Liu, Li, Li, Tao, Li, Chang-cheng, He, Li-hui, Zhu, Yi-bo, Song, Ying-jie, Liu, Huan-xiang, Bao, Rui
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2021; Elsevier
• Subjects: acyl coenzyme A; Crotonase; Crystal structure; Crystallography, X-Ray; Dynamic simulation; Enoyl-CoA Hydratase - chemistry; Enoyl-CoA Hydratase - metabolism; Humans; isomerases; moieties; molecular dynamics; Molecular Dynamics Simulation; Protein Conformation; Protein Conformation, alpha-Helical; Pseudomonas aeruginosa; Pseudomonas aeruginosa - chemistry; Pseudomonas aeruginosa - enzymology; Pseudomonas aeruginosa - metabolism; Pseudomonas Infections - microbiology; thioesters; X-ray diffraction; QS; TSA; Crotonase; ECI; RMSD; DCI; ECH; PCA; CS; OdaA; SSRF; CoA; DSF; MD; IPTG; Dynamic simulation; Pseudomonas aeruginosa; Crystal structure; P. aeruginosa

Crotonase superfamily members exhibit great catalytic diversity towards various acyl-CoA substrates. A common CoA moiety binding pattern is usually observed in this family, understanding the substrate-binding mechanism would facilitate the rational engineering of crotonases for improved properties....