User:Lori Wetmore/Sandbox 4
From Proteopedia
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ABC transporters are of particular medical interest, as they may contribute to the pathogenicity and drug resistance of pathogenic bacteria and some cancers.<ref name="Davidson">PMID:18535149</ref> | ABC transporters are of particular medical interest, as they may contribute to the pathogenicity and drug resistance of pathogenic bacteria and some cancers.<ref name="Davidson">PMID:18535149</ref> | ||
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=='''General ABC Structure'''== | =='''General ABC Structure'''== | ||
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=='''ABC Exporters'''== | =='''ABC Exporters'''== | ||
Revision as of 02:08, 27 September 2010
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| 2hyd, resolution 3.00Å () | |||||||||
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| Ligands: | , | ||||||||
| Gene: | SAV1866 (Staphylococcus aureus) | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Background Information
ATP-binding cassette (ABC) transporters are a superfamily of integral membrane proteins that harness the energy of ATP binding and hydrolysis to drive the trans-membrane movement of a variety of small molecules. ABC transporters function as homodimers, in which ATP binding and hydrolysis occurs in two sites that the interface of the nucleotide binding domains (NBD), while the paired transmembrane domains (TMD) facilitate substrate transport. Substrates may be imported or exported, depending upon the structure of the transporter. In ABC importers, which have only been found in prokaryotes, the NBD and TMD are separate polypeptides; however, in the ubiquitous exporters, the NBD and TMD are fused.
ABC transporters are of particular medical interest, as they may contribute to the pathogenicity and drug resistance of pathogenic bacteria and some cancers.[1]
General ABC Structure
ABC Exporters
Type I ABC Importers
Type II ABC Importers
References
- ↑ Davidson AL, Dassa E, Orelle C, Chen J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev. 2008 Jun;72(2):317-64, table of contents. PMID:18535149 doi:10.1128/MMBR.00031-07
