3ne5

Crystal structure of the CusBA heavy-metal efflux complex from Escherichia coli

spinqualitylabelsall models 3ne5, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ne5 is a 3 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: cusB, ylcD, b0574, JW0563 (ECOLI), cusA, ybdE, b0575, JW0564 (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CUSB_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. [CUSA_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. Publication Abstract from PubMed Gram-negative bacteria, such as Escherichia coli, expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membrane. The three parts are an inner membrane, substrate-binding transporter; a membrane fusion protein; and an outer-membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. A crystallographic model of this tripartite efflux complex has been unavailable because co-crystallization of the various components of the system has proven to be extremely difficult. We previously described the crystal structures of both the inner membrane transporter CusA and the membrane fusion protein CusB of the CusCBA efflux system of E. coli. Here we report the co-crystal structure of the CusBA efflux complex, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. The six CusB molecules seem to form a continuous channel. The affinity of the CusA and CusB interaction was found to be in the micromolar range. Finally, we have predicted a three-dimensional structure for the trimeric CusC outer membrane channel and developed a model of the tripartite efflux assemblage. This CusC(3)-CusB(6)-CusA(3) model shows a 750-kilodalton efflux complex that spans the entire bacterial cell envelope and exports Cu I and Ag I ions. Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.,Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, Yu EW Nature. 2011 Feb 24;470(7335):558-62. PMID:21350490 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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