View source for 4c2f


==Crystal structure of the CtpB R168A mutant present in an active conformation==
<StructureSection load='4c2f' size='340' side='right'caption='[[4c2f]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4c2f]] is a 3 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=4C2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C2F FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4c2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c2f OCA], [https://pdbe.org/4c2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c2f RCSB], [https://www.ebi.ac.uk/pdbsum/4c2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c2f ProSAT]</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 ==
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<ref>PMID:24243021</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c2f" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Escherichia coli BL21]]
[[Category: Large Structures]]
[[Category: Clausen T]]
[[Category: Heuck A]]
[[Category: Kurzbauer R]]
[[Category: Mastny M]]