View source for 4u64


==Structure of the periplasmic output domain of the Legionella pneumophila LapD ortholog CdgS9 in the apo state==
<StructureSection load='4u64' size='340' side='right'caption='[[4u64]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4u64]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U64 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]] 2.141&#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=4u64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u64 OCA], [https://pdbe.org/4u64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u64 RCSB], [https://www.ebi.ac.uk/pdbsum/4u64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u64 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5ZXA3_LEGPH Q5ZXA3_LEGPH] 
<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>
<div class="pdbe-citations 4u64" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
[[Category: Boyd CD]]
[[Category: Chatterjee D]]
[[Category: Cooley RB]]
[[Category: Mehl RA]]
[[Category: O'Toole GA]]
[[Category: Sondermann HS]]