1lsu

From Proteopedia

(Difference between revisions)

Revision as of 14:51, 27 October 2021

KTN Bsu222 Crystal Structure in Complex with NADH

Structural highlights

1lsu is a 2 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1lss
Gene:	KtrA ("Vibrio subtilis" Ehrenberg 1835)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KTRA_BACSU] Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The regulation of cation content is critical for cell growth. However, the molecular mechanisms that gate the systems that control K+ movements remain unclear. KTN is a highly conserved cytoplasmic domain present ubiquitously in a variety of prokaryotic and eukaryotic K+ channels and transporters. Here we report crystal structures for two representative KTN domains that reveal a dimeric hinged assembly. Alternative ligands NAD+ and NADH block or vacate, respectively, the hinge region affecting the dimer's conformational flexibility. Conserved, surface-exposed hydrophobic patches that become coplanar upon hinge closure provide an assembly interface for KTN tetramerization. Mutational analysis using the KefC system demonstrates that this domain directly interacts with its respective transmembrane constituent, coupling ligand-mediated KTN conformational changes to the permease's activity.

A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch.,Roosild TP, Miller S, Booth IR, Choe S Cell. 2002 Jun 14;109(6):781-91. PMID:12086676^[2]

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

References

↑ Holtmann G, Bakker EP, Uozumi N, Bremer E. KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity. J Bacteriol. 2003 Feb;185(4):1289-98. PMID:12562800
↑ Roosild TP, Miller S, Booth IR, Choe S. A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell. 2002 Jun 14;109(6):781-91. PMID:12086676

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lsu"

@@ Line 3: / Line 3: @@
 <StructureSection load='1lsu' size='340' side='right'caption='[[1lsu]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lsu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LSU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lsu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSU FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lss|1lss]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KtrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KtrA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsu OCA], [http://pdbe.org/1lsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lsu RCSB], [http://www.ebi.ac.uk/pdbsum/1lsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsu ProSAT]</span></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=1lsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsu OCA], [https://pdbe.org/1lsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsu RCSB], [https://www.ebi.ac.uk/pdbsum/1lsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KTRA_BACSU KTRA_BACSU]] Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.<ref>PMID:12562800</ref>
+[[https://www.uniprot.org/uniprot/KTRA_BACSU KTRA_BACSU]] Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.<ref>PMID:12562800</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1lsu

From Proteopedia

Revision as of 14:51, 27 October 2021

KTN Bsu222 Crystal Structure in Complex with NADH

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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