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| | <StructureSection load='3w45' size='340' side='right'caption='[[3w45]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='3w45' size='340' side='right'caption='[[3w45]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w45]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W45 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w45]] is a 2 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=3W45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W45 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w40|3w40]], [[3w41|3w41]], [[3w42|3w42]], [[3w43|3w43]], [[3w44|3w44]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU04740, rsbX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </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=3w45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w45 OCA], [https://pdbe.org/3w45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w45 RCSB], [https://www.ebi.ac.uk/pdbsum/3w45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w45 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=3w45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w45 OCA], [https://pdbe.org/3w45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w45 RCSB], [https://www.ebi.ac.uk/pdbsum/3w45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w45 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU]] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref>
| + | [https://www.uniprot.org/uniprot/RSBX_BACSU RSBX_BACSU] Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.<ref>PMID:1592822</ref> <ref>PMID:8468294</ref> <ref>PMID:8824586</ref> <ref>PMID:9658013</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | In the general stress response of Bacillus subtilis, which is governed by the sigma factor sigma(B), stress signalling is relayed by a cascade of Rsb proteins that regulate sigma(B) activity. RsbX, a PPM II phosphatase, halts the response by dephosphorylating the stressosome composed of RsbR and RsbS. The crystal structure of RsbX reveals a reorganization of the catalytic centre, with the second Mn(2+) ion uniquely coordinated by Gly47 O from the beta4-alpha1 loop instead of a water molecule as in PPM I phosphatases. An extra helical turn of alpha1 tilts the loop towards the metal-binding site, and the beta2-beta3 loop swings outwards to accommodate this tilting. The residues critical for this defining feature of the PPM II phosphatases are highly conserved. Formation of the catalytic centre is metal-specific, as crystallization with Mg(2+) ions resulted in a shift of the beta4-alpha1 loop that led to loss of the second ion. RsbX also lacks the flap subdomain characteristic of PPM I phosphatases. On the basis of a stressosome model, the activity of RsbX towards RsbR-P and RsbS-P may be influenced by the different accessibilities of their phosphorylation sites.
| + | |
| - | | + | |
| - | Structure of the RsbX phosphatase involved in the general stress response of Bacillus subtilis.,Teh AH, Makino M, Hoshino T, Baba S, Shimizu N, Yamamoto M, Kumasaka T Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1392-9. doi:, 10.1107/S1399004715007166. Epub 2015 May 23. PMID:26057679<ref>PMID:26057679</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3w45" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoserine phosphatase]]
| + | [[Category: Baba S]] |
| - | [[Category: Baba, S]] | + | [[Category: Kumasaka T]] |
| - | [[Category: Kumasaka, T]] | + | [[Category: Makino M]] |
| - | [[Category: Makino, M]] | + | [[Category: Shimizu N]] |
| - | [[Category: Shimizu, N]] | + | [[Category: Teh AH]] |
| - | [[Category: Teh, A H]] | + | [[Category: Yamamoto M]] |
| - | [[Category: Yamamoto, M]] | + | |
| - | [[Category: Alpha-beta beta-alpha sandwich fold]]
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| - | [[Category: Dephosphorylation]]
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| - | [[Category: Environmental stress]]
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| - | [[Category: Gene expression regulation]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Magnesium/manganese binding]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Phosphoric monoester hydrolase]]
| + | |
| - | [[Category: Protein phosphatase]]
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| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Stressosome]]
| + | |
| - | [[Category: Tertiary]]
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