2W1B

The structure of the efflux pump AcrB in complex with bile acid

Summary for 2W1B

Entry DOI	10.2210/pdb2w1b/pdb
Related	1IWG 1OY6 1OY8 1OY9 1OYD 1OYE 1T9T 1T9U 1T9V 1T9W 1T9X 1T9Y 2GIF 2HRT 2J8S
Descriptor	ACRIFLAVIN RESISTANCE PROTEIN B, (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID (2 entities in total)
Functional Keywords	membrane protein, multidrug efflux, membrane, transport, transporter
Biological source	ESCHERICHIA COLI
Cellular location	Cell inner membrane; Multi-pass membrane protein: P31224
Total number of polymer chains	1
Total formula weight	114057.75
Authors	Drew, D.,Klepsch, M.M.,Newstead, S.,Flaig, R.,De Gier, J.W.,Iwata, S.,Beis, K. (deposition date: 2008-10-17, release date: 2008-12-09, Last modification date: 2023-12-13)
Primary citation	Drew, D.,Klepsch, M.M.,Newstead, S.,Flaig, R.,De Gier, J.W.,Iwata, S.,Beis, K. The Structure of the Efflux Pump Acrb in Complex with Bile Acid. Mol.Membr.Biol., 25:677-, 2008 Cited by PubMed Abstract: Gastrointestinal bacteria, like Escherichia coli, must remove bile acid to survive in the gut. Bile acid removal in E. coli is thought to be mediated primarily by the multidrug efflux pump, AcrB. Here, we present the structure of E. coli AcrB in complex with deoxycholate at 3.85 A resolution. All evidence suggests that bile acid is transported out of the cell via the periplasmic vestibule of the AcrAB-TolC complex. PubMed: 19023693 DOI: 10.1080/09687680802552257 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.85 Å)

Structure validation