3EYW

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

Summary for 3EYW

• Entry DOI: 10.2210/pdb3eyw/pdb
• Descriptor: C-terminal domain of Glutathione-regulated potassium-efflux system protein kefC fused to full length Glutathione-regulated potassium-efflux system ancillary protein kefF, FLAVIN MONONUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: ktn, rck, k+ channel, k+ transport, kefc, k+ efflux, channel regulation, antiport, inner membrane, ion transport, membrane, potassium, potassium transport, transmembrane, transport protein
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : P0A754
• Total number of polymer chains: 2
• Total formula weight: 95510.35

Authors

Roosild, T.P. (deposition date: 2008-10-22, release date: 2009-06-30, Last modification date: 2023-09-06)

Primary citation

Roosild, T.P.,Castronovo, S.,Miller, S.,Li, C.,Rasmussen, T.,Bartlett, W.,Gunasekera, B.,Choe, S.,Booth, I.R.
KTN (RCK) Domains Regulate K(+) Channels and Transporters by Controlling the Dimer-Hinge Conformation.
Structure, 17:893-903, 2009

PubMed Abstract: 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.

PubMed: 19523906
DOI: 10.1016/j.str.2009.03.018

Experimental method

X-RAY DIFFRACTION (2.4 Å)