The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation.
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&quo...
Main Authors: | Jingwei Weng, Kangnian Fan, Wenning Wang |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2012-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3260306?pdf=render |
Similar Items
-
ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.
by: Chao Pan, et al.
Published: (2016-01-01) -
Structural and Biochemical Characterization of the Vitamin B₁₂ ABC Transporter, BtuCD-F
by: Borths, Elizabeth Loraine
Published: (2005) -
Conformational Motions and Functionally Key Residues for Vitamin B12 Transporter BtuCD–BtuF Revealed by Elastic Network Model with a Function-Related Internal Coordinate
by: Ji-Guo Su, et al.
Published: (2015-08-01) -
Single-molecule visualization of conformational changes and substrate transport in the vitamin B12 ABC importer BtuCD-F
by: Joris M. H. Goudsmits, et al.
Published: (2017-11-01) -
The Molecular Mechanism of the Escherichia Coli vitamin B12 Transporter BtuCD-F: Real-time Observation of the Transporter in Motion
by: Kim, Jinrang
Published: (2012)