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• W2004453704 endingPage "e30465" @default.
• W2004453704 startingPage "e30465" @default.
• W2004453704 abstract "BtuCD is a member of the ATP-binding cassette transporters in Escherichia coli that imports vitamin B(12) into the cell by utilizing the energy of ATP hydrolysis. Crystal structures of BtuCD and its homologous protein HI1470/1 in various conformational states support the alternating access mechanism which proposes the conformational transitions of the substrate translocation pathway at transmembrane domain (TMD) between the outward-facing and inward-facing states. The conformational transition at TMD is assumed to couple with the movement of the cytoplasmic nucleotide-binding domains (NBDs) driven by ATP hydrolysis/binding. In this study, we performed targeted molecular dynamics (MD) simulations to explore the atomic details of the conformational transitions of BtuCD importer. The outward-facing to inward-facing (O→I) transition was found to be initiated by the conformational movement of NBDs. The subsequent reorientation of the substrate translocation pathway at TMD began with the closing of the periplasmic gate, followed by the opening of the cytoplamic gate in the last stage of the conformational transition due to the extensive hydrophobic interactions at this region, consistent with the functional requirement of unidirectional transport of the substrates. The reverse inward-facing to outward-facing (I→O) transition was found to exhibit intrinsic diversity of the conformational transition pathways and significant structural asymmetry, suggesting that the asymmetric crystal structure of BtuCD-F is an intermediate state in this process." @default.
• W2004453704 created "2016-06-24" @default.
• W2004453704 creator A5002073070 @default.
• W2004453704 creator A5039234406 @default.
• W2004453704 creator A5050394964 @default.
• W2004453704 date "2012-01-17" @default.
• W2004453704 modified "2023-10-18" @default.
• W2004453704 title "The Conformational Transition Pathways of ATP-Binding Cassette Transporter BtuCD Revealed by Targeted Molecular Dynamics Simulation" @default.
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• W2004453704 doi "https://doi.org/10.1371/journal.pone.0030465" @default.
• W2004453704 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3260306" @default.
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• W2004453704 hasPublicationYear "2012" @default.
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