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

Experimental method

X-RAY DIFFRACTION (2.4 Å)