4u64: Difference between revisions

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u64 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u64 RCSB], [http://www.ebi.ac.uk/pdbsum/4u64 PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

Stable surface adhesion of cells is one of the early pivotal steps in bacterial biofilm formation, a prevalent adaptation strategy in response to changing environments. In Pseudomonas fluorescens, this process is regulated by the Lap system and the second messenger cyclic-di-GMP. High cytoplasmic levels of cyclic-di-GMP activate the transmembrane receptor LapD that in turn recruits the periplasmic protease LapG, preventing it from cleaving a cell surface-bound adhesin, thereby promoting cell adhesion. In this study, we elucidate the molecular basis of LapG regulation by LapD and reveal a remarkably sensitive switching mechanism that is controlled by LapD's HAMP domain. LapD appears to act as a coincidence detector, whereby a weak interaction of LapG with LapD transmits a transient outside-in signal that is reinforced only when cyclic-di-GMP levels increase. Given the conservation of key elements of this receptor system in many bacterial species, the results are broadly relevant for cyclic-di-GMP- and HAMP domain-regulated transmembrane signaling.DOI: http://dx.doi.org/10.7554/eLife.03650.001.

Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP.,Chatterjee D, Cooley RB, Boyd CD, Mehl RA, O'Toole GA, Sondermann H Elife. 2014 Sep 2;3:e03650. doi: 10.7554/eLife.03650. PMID:25182848<ref>PMID:25182848</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 7: / Line 7: @@
 <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4u64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u64 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u64 RCSB], [http://www.ebi.ac.uk/pdbsum/4u64 PDBsum]</span></td></tr>
 <table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Stable surface adhesion of cells is one of the early pivotal steps in bacterial biofilm formation, a prevalent adaptation strategy in response to changing environments. In Pseudomonas fluorescens, this process is regulated by the Lap system and the second messenger cyclic-di-GMP. High cytoplasmic levels of cyclic-di-GMP activate the transmembrane receptor LapD that in turn recruits the periplasmic protease LapG, preventing it from cleaving a cell surface-bound adhesin, thereby promoting cell adhesion. In this study, we elucidate the molecular basis of LapG regulation by LapD and reveal a remarkably sensitive switching mechanism that is controlled by LapD's HAMP domain. LapD appears to act as a coincidence detector, whereby a weak interaction of LapG with LapD transmits a transient outside-in signal that is reinforced only when cyclic-di-GMP levels increase. Given the conservation of key elements of this receptor system in many bacterial species, the results are broadly relevant for cyclic-di-GMP- and HAMP domain-regulated transmembrane signaling.DOI: http://dx.doi.org/10.7554/eLife.03650.001.
+Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP.,Chatterjee D, Cooley RB, Boyd CD, Mehl RA, O'Toole GA, Sondermann H Elife. 2014 Sep 2;3:e03650. doi: 10.7554/eLife.03650. PMID:25182848<ref>PMID:25182848</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>