3eff

From Proteopedia

(Difference between revisions)

Current revision

The Crystal Structure of Full-Length KcsA in its Closed Conformation

Structural highlights

3eff is a 8 chain structure with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCSA_STRLI Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).^[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

KcsA is a proton-activated, voltage-modulated K(+) channel that has served as the archetype pore domain in the Kv channel superfamily. Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic chaperones to determine the structure of full-length KcsA at 3.8 A, as well as that of its isolated C-terminal domain at 2.6 A. The structure of the full-length KcsA-Fab complex reveals a well-defined, 4-helix bundle that projects approximately 70 A toward the cytoplasm. This bundle promotes a approximately 15 degrees bending in the inner bundle gate, tightening its diameter and shifting the narrowest point 2 turns of helix below. Functional analysis of the full-length KcsA-Fab complex suggests that the C-terminal bundle remains whole during gating. We suggest that this structure likely represents the physiologically relevant closed conformation of KcsA.

Crystal structure of full-length KcsA in its closed conformation.,Uysal S, Vasquez V, Tereshko V, Esaki K, Fellouse FA, Sidhu SS, Koide S, Perozo E, Kossiakoff A Proc Natl Acad Sci U S A. 2009 Apr 3. PMID:19346472^[2]

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

References

↑ Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706
↑ Uysal S, Vasquez V, Tereshko V, Esaki K, Fellouse FA, Sidhu SS, Koide S, Perozo E, Kossiakoff A. Crystal structure of full-length KcsA in its closed conformation. Proc Natl Acad Sci U S A. 2009 Apr 3. PMID:19346472

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='3eff' size='340' side='right'caption='[[3eff]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3eff]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3EFF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3eff]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EFF FirstGlance]. <br>
-</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=3eff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eff OCA], [http://pdbe.org/3eff PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eff RCSB], [http://www.ebi.ac.uk/pdbsum/3eff PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eff ProSAT]</span></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]] 3.8&#8491;</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=3eff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eff OCA], [https://pdbe.org/3eff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eff RCSB], [https://www.ebi.ac.uk/pdbsum/3eff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eff ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI]] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
+[https://www.uniprot.org/uniprot/KCSA_STRLI KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).<ref>PMID:7489706</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 13: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/3eff_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 39: / Line 40: @@
 [[Category: Mus musculus]]
 [[Category: Streptomyces lividans]]
-[[Category: Esaki, K]]
+[[Category: Esaki K]]
-[[Category: Fellouse, F A]]
+[[Category: Fellouse FA]]
-[[Category: Koide, S]]
+[[Category: Koide S]]
-[[Category: Kossiakoff, A]]
+[[Category: Kossiakoff A]]
-[[Category: Perozo, E]]
+[[Category: Perozo E]]
-[[Category: Sidhu, S S]]
+[[Category: Sidhu SS]]
-[[Category: Tereshko, T]]
+[[Category: Tereshko T]]
-[[Category: Uysal, S]]
+[[Category: Uysal S]]
-[[Category: Vasquez, V]]
+[[Category: Vasquez V]]
-[[Category: Bulge helix]]
-[[Category: Cell membrane]]
-[[Category: Full length kcsa]]
-[[Category: Ion transport]]
-[[Category: Ionic channel]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Voltage-gated channel]]

3eff

From Proteopedia

Current revision

The Crystal Structure of Full-Length KcsA in its Closed Conformation

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox