2hmw

From Proteopedia

(Difference between revisions)

Current revision

Square-shaped octameric ring structure of an RCK domain with ATP bound

Structural highlights

2hmw is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:
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 KtrAB ion transporter is a complex of the KtrB membrane protein and KtrA, an RCK domain. RCK domains regulate eukaryotic and prokaryotic membrane proteins involved in K(+) transport. Conflicting functional models have proposed two different oligomeric arrangements for RCK domains, tetramer versus octamer. Our results for the KtrAB RCK domain clearly show an octamer in solution and in the crystal. We determined the structure of this protein in three different octameric ring conformations that resemble the RCK-domain octamer observed in the MthK potassium channel but show striking differences in size and symmetry. We present experimental evidence for the association between one RCK octameric ring and two KtrB membrane proteins. These results provide insights into the quaternary organization of the KtrAB transporter and its mechanism of activation and show that the RCK-domain octameric ring model is generally applicable to other ion-transport systems.

The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring.,Albright RA, Ibar JL, Kim CU, Gruner SM, Morais-Cabral JH Cell. 2006 Sep 22;126(6):1147-59. PMID:16990138^[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
↑ Albright RA, Ibar JL, Kim CU, Gruner SM, Morais-Cabral JH. The RCK domain of the KtrAB K+ transporter: multiple conformations of an octameric ring. Cell. 2006 Sep 22;126(6):1147-59. PMID:16990138 doi:10.1016/j.cell.2006.08.028

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/2hmw"

Categories: Bacillus subtilis | Large Structures | Albright RA | Morais-Cabral JH

@@ Line 1: / Line 1: @@
 ==Square-shaped octameric ring structure of an RCK domain with ATP bound==
-<StructureSection load='2hmw' size='340' side='right' caption='[[2hmw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='2hmw' size='340' side='right'caption='[[2hmw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hmw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HMW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hmw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HMW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lsu|1lsu]], [[1lss|1lss]], [[1lnq|1lnq]], [[2hmt|2hmt]], [[2hmu|2hmu]], [[2hmv|2hmv]], [[2hms|2hms]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yuaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2hmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmw OCA], [https://pdbe.org/2hmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hmw RCSB], [https://www.ebi.ac.uk/pdbsum/2hmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmw ProSAT]</span></td></tr>
-<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=2hmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmw OCA], [http://pdbe.org/2hmw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hmw RCSB], [http://www.ebi.ac.uk/pdbsum/2hmw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hmw 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/2hmw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/2hmw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus globigii migula 1900]]
+[[Category: Bacillus subtilis]]
-[[Category: Albright, R A]]
+[[Category: Large Structures]]
-[[Category: Morais-Cabral, J H]]
+[[Category: Albright RA]]
-[[Category: Ion transporter]]
+[[Category: Morais-Cabral JH]]
-[[Category: Ktn]]
-[[Category: Ktr]]
-[[Category: Ktra]]
-[[Category: Ktrab]]
-[[Category: Membrane protein]]
-[[Category: Rck]]
-[[Category: Symporter]]
-[[Category: Transport protein]]

2hmw

From Proteopedia

Current revision

Square-shaped octameric ring structure of an RCK domain with ATP bound

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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