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| | <StructureSection load='4c2d' size='340' side='right'caption='[[4c2d]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4c2d' size='340' side='right'caption='[[4c2d]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c2d]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C2D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c2d]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168] and [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C2D FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c2c|4c2c]], [[4c2e|4c2e]], [[4c2f|4c2f]], [[4c2g|4c2g]], [[4c2h|4c2h]]</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]] 2.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/C-terminal_processing_peptidase C-terminal processing peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.102 3.4.21.102] </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=4c2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2d OCA], [https://pdbe.org/4c2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c2d RCSB], [https://www.ebi.ac.uk/pdbsum/4c2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2d 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=4c2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2d OCA], [http://pdbe.org/4c2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c2d RCSB], [http://www.ebi.ac.uk/pdbsum/4c2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTPB_BACSU CTPB_BACSU]] Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.<ref>PMID:14526016</ref> <ref>PMID:16818230</ref> <ref>PMID:17557826</ref> | + | [https://www.uniprot.org/uniprot/CTPB_BACSU CTPB_BACSU] Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.<ref>PMID:14526016</ref> <ref>PMID:16818230</ref> <ref>PMID:17557826</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: C-terminal processing peptidase]]
| + | [[Category: Escherichia coli BL21]] |
| - | [[Category: Escherichia coli]] | + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clausen, T]] | + | [[Category: Clausen T]] |
| - | [[Category: Heuck, A]] | + | [[Category: Heuck A]] |
| - | [[Category: Kurzbauer, R]] | + | [[Category: Kurzbauer R]] |
| - | [[Category: Mastny, M]] | + | [[Category: Mastny M]] |
| - | [[Category: Hydrolase-peptide complex]]
| + | |
| - | [[Category: Proteolytic tunnel]]
| + | |
| Structural highlights
Function
CTPB_BACSU Involved in the signal transduction pathway leading to the proteolytic activation of the mother cell transcription factor pro-sigma-K during sporulation. The signaling serine protease CtpB triggers pro-sigma-K processing by cleaving the regulatory protein SpoIVFA and is necessary for the proper timing of sigma-K activation.[1] [2] [3]
Publication Abstract from PubMed
Spore formation in Bacillus subtilis relies on a regulated intramembrane proteolysis (RIP) pathway that synchronizes mother-cell and forespore development. To address the molecular basis of this SpoIV transmembrane signaling, we carried out a structure-function analysis of the activating protease CtpB. Crystal structures reflecting distinct functional states show that CtpB constitutes a ring-like protein scaffold penetrated by two narrow tunnels. Access to the proteolytic sites sequestered within these tunnels is controlled by PDZ domains that rearrange upon substrate binding. Accordingly, CtpB resembles a minimal version of a self-compartmentalizing protease regulated by a unique allosteric mechanism. Moreover, biochemical analysis of the PDZ-gated channel combined with sporulation assays reveal that activation of the SpoIV RIP pathway is induced by the concerted activity of CtpB and a second signaling protease, SpoIVB. This proteolytic mechanism is of broad relevance for cell-cell communication, illustrating how distinct signaling pathways can be integrated into a single RIP module.
CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis.,Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T Cell. 2013 Oct 24;155(3):647-58. doi: 10.1016/j.cell.2013.09.050. Epub 2013 Oct, 24. PMID:24243021[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pan Q, Losick R, Rudner DZ. A second PDZ-containing serine protease contributes to activation of the sporulation transcription factor sigmaK in Bacillus subtilis. J Bacteriol. 2003 Oct;185(20):6051-6. PMID:14526016
- ↑ Campo N, Rudner DZ. A branched pathway governing the activation of a developmental transcription factor by regulated intramembrane proteolysis. Mol Cell. 2006 Jul 7;23(1):25-35. PMID:16818230 doi:http://dx.doi.org/10.1016/j.molcel.2006.05.019
- ↑ Campo N, Rudner DZ. SpoIVB and CtpB are both forespore signals in the activation of the sporulation transcription factor sigmaK in Bacillus subtilis. J Bacteriol. 2007 Aug;189(16):6021-7. Epub 2007 Jun 8. PMID:17557826 doi:http://dx.doi.org/10.1128/JB.00399-07
- ↑ Mastny M, Heuck A, Kurzbauer R, Heiduk A, Boisguerin P, Volkmer R, Ehrmann M, Rodrigues CD, Rudner DZ, Clausen T. CtpB Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling during Spore Formation in Bacillus subtilis. Cell. 2013 Oct 24;155(3):647-58. doi: 10.1016/j.cell.2013.09.050. Epub 2013 Oct, 24. PMID:24243021 doi:http://dx.doi.org/10.1016/j.cell.2013.09.050
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