3o0t

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==Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in complex with phosphate==
==Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in complex with phosphate==
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<StructureSection load='3o0t' size='340' side='right' caption='[[3o0t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3o0t' size='340' side='right'caption='[[3o0t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O0T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o0t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O0T FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mxo|3mxo]]</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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">PGAM5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3o0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0t OCA], [https://pdbe.org/3o0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o0t RCSB], [https://www.ebi.ac.uk/pdbsum/3o0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0t ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
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<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=3o0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o0t OCA], [http://pdbe.org/3o0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o0t RCSB], [http://www.ebi.ac.uk/pdbsum/3o0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o0t ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PGAM5_HUMAN PGAM5_HUMAN]] Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore.<ref>PMID:18387606</ref> <ref>PMID:19590015</ref> <ref>PMID:22265414</ref>
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[https://www.uniprot.org/uniprot/PGAM5_HUMAN PGAM5_HUMAN] Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore.<ref>PMID:18387606</ref> <ref>PMID:19590015</ref> <ref>PMID:22265414</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/3o0t_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/3o0t_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3o0t ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3o0t ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N-terminal regulatory sequences, providing a model for structural plasticity, dimerization of the catalytic domain, and the assembly into an enzymatically active dodecameric form. Oligomeric states observed in structures were supported by hydrogen exchange mass spectrometry, size-exclusion chromatography, and analytical ultracentrifugation experiments in solution. We report that the catalytically important N-terminal WDPNWD motif acts as a structural integrator assembling PGAM5 into a dodecamer, allosterically activating the phosphatase by promoting an ordering of the catalytic loop. Additionally the observed active site plasticity enabled visualization of essential conformational rearrangements of catalytic elements. The comprehensive biophysical characterization offers detailed structural models of this key mitochondrial phosphatase that has been associated with the development of diverse diseases.
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Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly.,Chaikuad A, Filippakopoulos P, Marcsisin SR, Picaud S, Schroder M, Sekine S, Ichijo H, Engen JR, Takeda K, Knapp S Structure. 2017 Jul 5;25(7):1089-1099.e3. doi: 10.1016/j.str.2017.05.020. Epub, 2017 Jun 22. PMID:28648608<ref>PMID:28648608</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 3o0t" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Phosphoglycerate Mutase|Phosphoglycerate Mutase]]
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*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
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*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Alfano, I]]
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[[Category: Alfano I]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Barr, A]]
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[[Category: Barr A]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Chaikuad, A]]
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[[Category: Chaikuad A]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Filippakopoulos P]]
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[[Category: Filippakopoulos, P]]
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[[Category: Ichijo H]]
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[[Category: Ichijo, H]]
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[[Category: Knapp S]]
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[[Category: Knapp, S]]
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[[Category: Picaud S]]
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[[Category: Picaud, S]]
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[[Category: Takeda K]]
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[[Category: Structural genomic]]
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[[Category: Weigelt J]]
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[[Category: Takeda, K]]
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[[Category: Von Delft F]]
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[[Category: Weigelt, J]]
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[[Category: Bxlbv68]]
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[[Category: Hydrolase]]
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[[Category: Mgc5352 protein]]
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[[Category: Mitochondrial protein]]
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[[Category: Pgam5]]
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[[Category: Phosphoglycerate mutase family member 5]]
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[[Category: Serine/threonine phosphatase]]
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[[Category: Sgc]]
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Current revision

Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5) in complex with phosphate

PDB ID 3o0t

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