Molecular dynamics simulation of the transmembrane subunit of BtuCD in the lipid bilayer

• Published in: Science China. Life sciences Vol. 53; no. 5; pp. 620 - 630
• Main Authors: Sun, TingGuang, Liu, Ming, Chen, WeiZu, Wang, CunXin
• Format: Journal Article
• Language: English
• Published: Beijing Science China Press 01.05.2010; Springer Nature B.V
• Subjects: ATP-Binding Cassette Transporters - chemistry; Biomedical and Life Sciences; Crystal structure; Escherichia coli; Escherichia coli Proteins - chemistry; Life Sciences; Lipid Bilayers - chemistry; Models, Molecular; Molecular Dynamics Simulation; Principal Component Analysis; Research Papers; Vitamin B 12 - metabolism; functional motion; BtuCD; principal component analysis; POPC
• ISSN: 1674-7305; 1869-1889
• DOI: 10.1007/s11427-010-0103-7

Based on the crystal structure of the vitamin B 12 transporter protein of Escherichia coli (BtuCD) a system consisting of the BtuCD transmembrane domain (BtuC) and the palmitoyloleoyl phosphatidylcholine (POPC) lipid bilayer was constructed in silica , and a more-than-57-nanosecond molecular dynamics (MD) simulation was performed on it to reveal the intrinsic functional motions of BtuC. The results showed that a stable protein-lipid bilayer was obtained and the POPC lipid bilayer was able to adjust its thickness to match the embedded BtuC which underwent relatively complicated motions. These results may help to understand the mechanism of transmembrane substrate transport at the atomic level.