4c2d: Difference between revisions
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==Crystal structure of the protease CtpB in an active state== | |||
<StructureSection load='4c2d' size='340' side='right' caption='[[4c2d]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== 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> | |||
</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> | |||
<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'>[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://www.rcsb.org/pdb/explore.do?structureId=4c2d RCSB], [http://www.ebi.ac.uk/pdbsum/4c2d PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacsu]] | |||
[[Category: C-terminal processing peptidase]] | [[Category: C-terminal processing peptidase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[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: Hydrolase-peptide complex]] | ||
[[Category: Proteolytic tunnel]] | [[Category: Proteolytic tunnel]] | ||
