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4c2e

From Proteopedia

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Current revision

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

Structural highlights

4c2e is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4c2e"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the protease CtpB(S309A) present in a resting state==
-<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 ==
-<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>
+<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>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=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>
-<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://www.rcsb.org/pdb/explore.do?structureId=4c2e RCSB], [http://www.ebi.ac.uk/pdbsum/4c2e PDBsum]</span></td></tr>
 </table>
+== Function ==
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4c2e" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacsu]]
+[[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: C-terminal processing peptidase]]
+[[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]]
-[[Category: Proteolytic tunnel]]

4c2e

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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