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4c2e

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<StructureSection load='4c2e' size='340' side='right'caption='[[4c2e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4c2e' size='340' side='right'caption='[[4c2e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c2e]] is a 2 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=4C2E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C2E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c2e]] 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=4C2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C2E FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c2c|4c2c]], [[4c2d|4c2d]], [[4c2f|4c2f]], [[4c2g|4c2g]], [[4c2h|4c2h]]</td></tr>
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</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=4c2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2e OCA], [https://pdbe.org/4c2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c2e RCSB], [https://www.ebi.ac.uk/pdbsum/4c2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2e ProSAT]</span></td></tr>
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<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>
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<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=4c2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2e OCA], [http://pdbe.org/4c2e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c2e RCSB], [http://www.ebi.ac.uk/pdbsum/4c2e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2e ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:24243021</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4c2e" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacsu]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: C-terminal processing peptidase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Clausen, T]]
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[[Category: Clausen T]]
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[[Category: Heuck, A]]
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[[Category: Heuck A]]
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[[Category: Kurzbauer, R]]
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[[Category: Kurzbauer R]]
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[[Category: Mastny, M]]
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[[Category: Mastny M]]
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[[Category: Hydrolase]]
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[[Category: Proteolytic tunnel]]
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Revision as of 17:21, 7 September 2022

Crystal structure of the protease CtpB(S309A) present in a resting state

PDB ID 4c2e

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