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ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF
- Source :
- FEBS Letters. 564:264-268
- Publication Year :
- 2004
- Publisher :
- Wiley, 2004.
-
Abstract
- ABC transporters are ubiquitous membrane proteins that facilitate unidirectional substrate translocation across the lipid bilayer. Over the past five years, new crystal structures have advanced our understanding of how ABC transporters couple adenosine triphosphate (ATP) hydrolysis to substrate transport. In the following, we will briefly review the results of these structural investigations and outline their mechanistic implications.
- Subjects :
- Models, Molecular
Protein Conformation
Biophysics
ATP-binding cassette transporter
Crystal structure
Biology
Crystallography, X-Ray
Biochemistry
chemistry.chemical_compound
Adenosine Triphosphate
Protein structure
Structural Biology
Genetics
Lipid bilayer
Molecular Biology
ATP-binding domain of ABC transporters
Escherichia coli Proteins
Cell Biology
chemistry
Membrane protein
Periplasmic Binding Proteins
ATP-Binding Cassette Transporters
ABC transporter
Transport mechanism
Adenosine triphosphate
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 564
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....3e4f024f04725b08106c6bcbe59c94a6
- Full Text :
- https://doi.org/10.1016/s0014-5793(04)00289-3