3eyw

Crystal structure of the C-terminal domain of E. coli KefC in complex with KefF

spinqualitylabelsall models 3eyw, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3eyw is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMN, MG, NAD, ZN Gene: kefC, trkC and kefF, yabF (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KEFC_ECOLI] Transport system that facilitates potassium-efflux, possibly by potassium-proton antiport. Publication Abstract from PubMed KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize the conductive state. The structure of the complex and functional analysis of KefC variants reveal that control of the conformational flexibility inherent in the KTN dimer hinge is modulated by KefF and essential for regulation of KefC ion flux. KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation.,Roosild TP, Castronovo S, Miller S, Li C, Rasmussen T, Bartlett W, Gunasekera B, Choe S, Booth IR Structure. 2009 Jun 10;17(6):893-903. PMID:19523906 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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