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| <StructureSection load='3t91' size='340' side='right'caption='[[3t91]], [[Resolution|resolution]] 2.64Å' scene=''> | | <StructureSection load='3t91' size='340' side='right'caption='[[3t91]], [[Resolution|resolution]] 2.64Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3t91]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T91 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t91]] 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=3T91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T91 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GL0:BETA-D-GULOPYRANOSE'>GL0</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.64Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t9q|3t9q]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GL0:BETA-D-GULOPYRANOSE'>GL0</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU00640, spoIIE, spoIIH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr> | + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://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=3t91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t91 OCA], [https://pdbe.org/3t91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t91 RCSB], [https://www.ebi.ac.uk/pdbsum/3t91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t91 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=3t91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t91 OCA], [https://pdbe.org/3t91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t91 RCSB], [https://www.ebi.ac.uk/pdbsum/3t91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t91 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[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.
| + | [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;">
| + | |
- | == Publication Abstract from PubMed ==
| + | |
- | Sporulation in Bacillus subtilis begins with an asymmetric cell division producing two genetically identical cells with different fates. SpoIIE is a membrane protein that localizes to the polar cell division sites where it causes FtsZ to relocate from mid-cell to form polar Z-rings. Following polar septation, SpoIIE establishes compartment-specific gene expression in the smaller forespore cell by dephosphorylating the anti-sigma factor antagonist SpoIIAA, leading to the release of the RNA polymerase sigma factor sigma(F) from an inhibitory complex with the anti-sigma factor SpoIIAB. SpoIIE therefore couples morphological development to differential gene expression. Here, we determined the crystal structure of the phosphatase domain of SpoIIE to 2.6 A spacing, revealing a domain-swapped dimer. SEC-MALLS (size-exclusion chromatography with multi-angle laser light scattering) analysis however suggested a monomer as the principal form in solution. A model for the monomer was derived from the domain-swapped dimer in which 2 five-stranded beta-sheets are packed against one another and flanked by alpha-helices in an alphabetabetaalpha arrangement reminiscent of other PP2C-type phosphatases. A flap region that controls access of substrates to the active site in other PP2C phosphatases is diminished in SpoIIE, and this observation correlates with the presence of a single manganese ion in the active site of SpoIIE in contrast to the two or three metal ions present in other PP2C enzymes. Mapping of a catalogue of mutational data onto the structure shows a clustering of sites whose point mutation interferes with the proper coupling of asymmetric septum formation to sigma factor activation and identifies a surface involved in intramolecular signaling.
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- | Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis.,Levdikov VM, Blagova EV, Rawlings AE, Jameson K, Tunaley J, Hart DJ, Barak I, Wilkinson AJ J Mol Biol. 2011 Nov 15. PMID:22115775<ref>PMID:22115775</ref>
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
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- | <div class="pdbe-citations 3t91" style="background-color:#fffaf0;"></div>
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- | == References ==
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- | <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Phosphoprotein phosphatase]]
| + | [[Category: Blagova EV]] |
- | [[Category: Blagova, E V]] | + | [[Category: Levdikov VM]] |
- | [[Category: Levdikov, V M]] | + | [[Category: Wilkinson AJ]] |
- | [[Category: Wilkinson, A J]] | + | |
- | [[Category: Dephosphorylating the anti-sigma factor antagonist spoiiaa]]
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- | [[Category: Hydrolase]]
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- | [[Category: Manganese binding]]
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- | [[Category: Phosphatase]]
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- | [[Category: Pp2c phosphatase domain]]
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- | [[Category: Spoiie]]
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- | [[Category: Sporulation]]
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