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090			_aB-14332
245	1	0	_aStructure and mechanism of the tripartite CusCBA heavy-metal efflux complex
490	0		_vPhil. Trans. R. Soc., 367(1592), p.1047-1058, 2012
520	3		_aGram-negative bacteria frequently expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membranes. The three parts are the inner membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (MFP, or adaptor); and an outer membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. One such efflux system CusCBA is responsible for extruding biocidal Cu(I)and Ag(I)ions. We previously described the crystal structures of both the inner membrane transporter CusA and the MFP CusB of Escherichia coli.We also determined the co-crystal structure of the CusBA adaptor-transporter efflux complex, showing that the transporter CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. Here, we summarize the structural information of these efflux proteins, and present the accumulated evidence that this efflux system uses methionine residues to bind and export Cu(I)and Ag(I). Genetic and structural analyses suggest that the CusA pump is capable of picking up the metal ions from both the periplasm and the cytoplasm. We propose a stepwise shuttle mechanism for this pump to export metal ions from the cell.
650	1	4	_aTRIPARTITE EFFLUX PUMP
650	1	4	_aMULTIDRUG RESISTANCE
650	1	4	_aRESISTANCE-NODULATION-CELL DIVISION
650	1	4	_aHEAVY-METAL EFFLUX
650	1	4	_aCUSCBA
650	1	4	_aX-RAY CRYSTALLOGRAPHY
700	1	2	_aLong, Feng
700	1	2	_aSu, C-C
700	1	2	_aLei, H-T
700	1	2	_aBolla, J.R.
700	1	2	_aDo, S.V.
700	1	2	_aYu, E.W.
856	4	0	_uhttps://drive.google.com/file/d/1-NsEqhP2-SO7L0P3f9cUT5dV4TbipOUO/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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