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| | <StructureSection load='3w40' size='340' side='right'caption='[[3w40]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='3w40' size='340' side='right'caption='[[3w40]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w40]] 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=3W40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W40 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w40]] 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=3W40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W40 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w41|3w41]], [[3w42|3w42]], [[3w43|3w43]], [[3w44|3w44]], [[3w45|3w45]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3w40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w40 OCA], [https://pdbe.org/3w40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w40 RCSB], [https://www.ebi.ac.uk/pdbsum/3w40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w40 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=3w40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w40 OCA], [https://pdbe.org/3w40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w40 RCSB], [https://www.ebi.ac.uk/pdbsum/3w40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w40 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;"> | | <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: 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]]
| + | |
| - | [[Category: Dephosphorylation]]
| + | |
| - | [[Category: Environmental stress]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Magnesium/manganese binding]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| - | [[Category: Phosphoric monoester hydrolase]]
| + | |
| - | [[Category: Protein phosphatase]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Stressosome]]
| + | |
| - | [[Category: Tertiary]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Boylan SA, Rutherford A, Thomas SM, Price CW. Activation of Bacillus subtilis transcription factor sigma B by a regulatory pathway responsive to stationary-phase signals. J Bacteriol. 1992 Jun;174(11):3695-706. PMID:1592822
- ↑ Benson AK, Haldenwang WG. Regulation of sigma B levels and activity in Bacillus subtilis. J Bacteriol. 1993 Apr;175(8):2347-56. PMID:8468294
- ↑ Yang X, Kang CM, Brody MS, Price CW. Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 1996 Sep 15;10(18):2265-75. PMID:8824586
- ↑ Smirnova N, Scott J, Voelker U, Haldenwang WG. Isolation and characterization of Bacillus subtilis sigB operon mutations that suppress the loss of the negative regulator RsbX. J Bacteriol. 1998 Jul;180(14):3671-80. PMID:9658013
- ↑ Teh AH, Makino M, Hoshino T, Baba S, Shimizu N, Yamamoto M, Kumasaka T. Structure of the RsbX phosphatase involved in the general stress response of Bacillus subtilis. Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1392-9. doi:, 10.1107/S1399004715007166. Epub 2015 May 23. PMID:26057679 doi:http://dx.doi.org/10.1107/S1399004715007166
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