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3eyw

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Revision as of 01:54, 25 December 2014

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

Structural highlights

3eyw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	kefC, trkC and kefF, yabF (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Roosild TP, Castronovo S, Miller S, Li C, Rasmussen T, Bartlett W, Gunasekera B, Choe S, Booth IR. KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation. Structure. 2009 Jun 10;17(6):893-903. PMID:19523906 doi:10.1016/j.str.2009.03.018

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3eyw"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3eyw RCSB], [http://www.ebi.ac.uk/pdbsum/3eyw PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KEFC_ECOLI KEFC_ECOLI]] Transport system that facilitates potassium-efflux, possibly by potassium-proton antiport.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3eyw

From Proteopedia

Revision as of 01:54, 25 December 2014

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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