3v0g

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Current revision (14:13, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3v0g' size='340' side='right'caption='[[3v0g]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3v0g' size='340' side='right'caption='[[3v0g]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v0g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascidia_intestinalis Ascidia intestinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V0G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v0g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ciona_intestinalis Ciona intestinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V0G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3v0d|3v0d]], [[3v0e|3v0e]], [[3v0f|3v0f]], [[3v0h|3v0h]], [[3v0i|3v0i]], [[3v0j|3v0j]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ci-VSP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7719 Ascidia intestinalis])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v0g OCA], [https://pdbe.org/3v0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v0g RCSB], [https://www.ebi.ac.uk/pdbsum/3v0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v0g 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=3v0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v0g OCA], [https://pdbe.org/3v0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v0g RCSB], [https://www.ebi.ac.uk/pdbsum/3v0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v0g ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q4W8A1_CIOIN Q4W8A1_CIOIN]
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The Ciona intestinalis voltage-sensing phosphatase (Ci-VSP) couples a voltage-sensing domain (VSD) to a lipid phosphatase that is similar to the tumor suppressor PTEN. How the VSD controls enzyme function has been unclear. Here, we present high-resolution crystal structures of the Ci-VSP enzymatic domain that reveal conformational changes in a crucial loop, termed the 'gating loop', that controls access to the active site by a mechanism in which residue Glu411 directly competes with substrate. Structure-based mutations that restrict gating loop conformation impair catalytic function and demonstrate that Glu411 also contributes to substrate selectivity. Structure-guided mutations further define an interaction between the gating loop and linker that connects the phosphatase to the VSD for voltage control of enzyme activity. Together, the data suggest that functional coupling between the gating loop and the linker forms the heart of the regulatory mechanism that controls voltage-dependent enzyme activation.
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A glutamate switch controls voltage-sensitive phosphatase function.,Liu L, Kohout SC, Xu Q, Muller S, Kimberlin CR, Isacoff EY, Minor DL Jr Nat Struct Mol Biol. 2012 May 6;19(6):633-41. doi: 10.1038/nsmb.2289. PMID:22562138<ref>PMID:22562138</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3v0g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ascidia intestinalis]]
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[[Category: Ciona intestinalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Isacoff, E Y]]
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[[Category: Isacoff EY]]
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[[Category: Kimberlin, C]]
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[[Category: Kimberlin C]]
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[[Category: Kohout, S C]]
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[[Category: Kohout SC]]
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[[Category: Liu, L]]
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[[Category: Liu L]]
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[[Category: Minor, D L]]
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[[Category: Minor DL]]
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[[Category: Muller, S]]
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[[Category: Muller S]]
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[[Category: Xu, Q]]
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[[Category: Xu Q]]
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[[Category: C2]]
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[[Category: Hydrolase]]
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[[Category: Phosphatase]]
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[[Category: Ptp]]
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Current revision

Crystal structure of Ciona intestinalis voltage sensor-containing phosphatase (Ci-VSP), residues 241-576(C363S), form III

PDB ID 3v0g

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OCA

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