3eyw

From Proteopedia

(Difference between revisions)

Current revision

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 K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KEFC_ECOLI Transport system that facilitates potassium-efflux, possibly by potassium-proton antiport.KEFF_ECOLI Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system.[HAMAP-Rule:MF_01414]^[1] ^[2] ^[3]

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^[4]

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

References

↑ Miller S, Ness LS, Wood CM, Fox BC, Booth IR. Identification of an ancillary protein, YabF, required for activity of the KefC glutathione-gated potassium efflux system in Escherichia coli. J Bacteriol. 2000 Nov;182(22):6536-40. PMID:11053405 doi:10.1128/JB.182.22.6536-6540.2000
↑ 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
↑ Lyngberg L, Healy J, Bartlett W, Miller S, Conway SJ, Booth IR, Rasmussen T. KefF, the regulatory subunit of the potassium efflux system KefC, shows quinone oxidoreductase activity. J Bacteriol. 2011 Sep;193(18):4925-32. PMID:21742892 doi:10.1128/JB.05272-11
↑ 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"

Categories: Escherichia coli K-12 | Large Structures | Roosild TP

@@ Line 3: / Line 3: @@
 <StructureSection load='3eyw' size='340' side='right'caption='[[3eyw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3eyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EYW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3eyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EYW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kefC, trkC and kefF, yabF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3eyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eyw OCA], [https://pdbe.org/3eyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eyw RCSB], [https://www.ebi.ac.uk/pdbsum/3eyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eyw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KEFC_ECOLI KEFC_ECOLI]] Transport system that facilitates potassium-efflux, possibly by potassium-proton antiport.
+[https://www.uniprot.org/uniprot/KEFC_ECOLI KEFC_ECOLI] Transport system that facilitates potassium-efflux, possibly by potassium-proton antiport.[https://www.uniprot.org/uniprot/KEFF_ECOLI KEFF_ECOLI] Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system.[HAMAP-Rule:MF_01414]<ref>PMID:11053405</ref> <ref>PMID:19523906</ref> <ref>PMID:21742892</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Roosild, T P]]
+[[Category: Roosild TP]]
-[[Category: Antiport]]
-[[Category: Channel regulation]]
-[[Category: Inner membrane]]
-[[Category: Ion transport]]
-[[Category: K+ channel]]
-[[Category: K+ efflux]]
-[[Category: K+ transport]]
-[[Category: Kefc]]
-[[Category: Ktn]]
-[[Category: Membrane]]
-[[Category: Potassium]]
-[[Category: Potassium transport]]
-[[Category: Rck]]
-[[Category: Transmembrane]]
-[[Category: Transport protein]]

3eyw

From Proteopedia

Current revision

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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