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| | <StructureSection load='5ucg' size='340' side='right'caption='[[5ucg]], [[Resolution|resolution]] 3.91Å' scene=''> | | <StructureSection load='5ucg' size='340' side='right'caption='[[5ucg]], [[Resolution|resolution]] 3.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ucg]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UCG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ucg]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UCG FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spoIIE, spoIIH, BSU00640 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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]] 3.906Å</td></tr> |
| - | <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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ucg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucg OCA], [https://pdbe.org/5ucg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ucg RCSB], [https://www.ebi.ac.uk/pdbsum/5ucg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucg 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=5ucg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ucg OCA], [http://pdbe.org/5ucg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ucg RCSB], [http://www.ebi.ac.uk/pdbsum/5ucg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ucg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SP2E_BACSU SP2E_BACSU]] Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation. | + | [https://www.uniprot.org/uniprot/SP2E_BACSU SP2E_BACSU] Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoprotein phosphatase]]
| + | [[Category: Bradshaw N]] |
| - | [[Category: Bradshaw, N]] | + | [[Category: Gaudet R]] |
| - | [[Category: Gaudet, R]] | + | [[Category: Levdikov V]] |
| - | [[Category: Levdikov, V]] | + | [[Category: Losick R]] |
| - | [[Category: Losick, R]] | + | [[Category: Wilkinson A]] |
| - | [[Category: Wilkinson, A]] | + | [[Category: Zimanyi C]] |
| - | [[Category: Zimanyi, C]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ppm phosphatase]]
| + | |
| Structural highlights
Function
SP2E_BACSU Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation.
Publication Abstract from PubMed
PP2C phosphatases control biological processes including stress responses, development, and cell division in all kingdoms of life. Diverse regulatory domains adapt PP2C phosphatases to specific functions, but how these domains control phosphatase activity was unknown. We present structures representing active and inactive states of the PP2C phosphatase SpoIIE from Bacillus subtilis. Based on structural analyses and genetic and biochemical experiments, we identify an alpha-helical switch that shifts a carbonyl oxygen into the active site to coordinate a metal cofactor. Our analysis indicates that this switch is widely conserved among PP2C family members, serving as a platform to control phosphatase activity in response to diverse inputs. Remarkably, the switch is shared with proteasomal proteases, which we identify as evolutionary and structural relatives of PP2C phosphatases. Although these proteases use an unrelated catalytic mechanism, rotation of equivalent helices controls protease activity by movement of the equivalent carbonyl oxygen into the active site.
A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.,Bradshaw N, Levdikov VM, Zimanyi CM, Gaudet R, Wilkinson AJ, Losick R Elife. 2017 May 20;6. pii: e26111. doi: 10.7554/eLife.26111. PMID:28527238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bradshaw N, Levdikov VM, Zimanyi CM, Gaudet R, Wilkinson AJ, Losick R. A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases. Elife. 2017 May 20;6. pii: e26111. doi: 10.7554/eLife.26111. PMID:28527238 doi:http://dx.doi.org/10.7554/eLife.26111
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