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A new dimer interface for an ABC transporter
- Source :
- International Journal of Antimicrobial Agents. 22:200-204
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- The crystallization of MsbA, an ATP-binding cassette (ABC) transporter involved in the transport of Lipid A in Escherichia coli, provided a fascinating glimpse into the high-resolution structure of an ABC transporter at 4.8 A. The E. coli crystal structure of MsbA reveals a dimer. Although the structure of the MsbA monomer is consistent with the biochemistry of ABC transporters, including the human multidrug resistance P-glycoprotein, the interface between the monomers in the MsbA dimer may not reflect the biologically relevant interface. We considered the interface in a two-armed MsbA dimer, named spiral. Our findings indicate that (i) the spiral MsbA dimer may have biological relevance for ABC transporters that interact with lipophilic substrates, and (ii) the dimer interface observed in the crystal structure of E. coli MsbA represents a crystallization artefact. A comparison of the spiral MsbA dimer with the recently published structure of MsbA in Vibrio cholera is also described.
- Subjects :
- Models, Molecular
Microbiology (medical)
Stereochemistry
Dimer
ATP-binding cassette transporter
Biology
medicine.disease_cause
MsbA dimer
chemistry.chemical_compound
Bacterial Proteins
medicine
Pharmacology (medical)
ATP Binding Cassette Transporter, Subfamily B, Member 1
Treatment resistance
Protein Structure, Quaternary
Escherichia coli
Binding Sites
Escherichia coli Proteins
Cryoelectron Microscopy
Transporter
General Medicine
Membrane transport
Protein Structure, Tertiary
Lipid A
Infectious Diseases
chemistry
ATP-Binding Cassette Transporters
Vibrio cholera
Crystallization
Dimerization
Subjects
Details
- ISSN :
- 09248579
- Volume :
- 22
- Database :
- OpenAIRE
- Journal :
- International Journal of Antimicrobial Agents
- Accession number :
- edsair.doi.dedup.....8c661ae360b76c77c673c76e9e3f08c3