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| | <StructureSection load='4u64' size='340' side='right'caption='[[4u64]], [[Resolution|resolution]] 2.14Å' scene=''> | | <StructureSection load='4u64' size='340' side='right'caption='[[4u64]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u64]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U64 FirstGlance]. <br> | + | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u65|4u65]]</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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg0829 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</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=4u64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u64 OCA], [http://pdbe.org/4u64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u64 RCSB], [http://www.ebi.ac.uk/pdbsum/4u64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u64 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5ZXA3_LEGPH Q5ZXA3_LEGPH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Legph]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Boyd, C D]] | + | [[Category: Boyd CD]] |
| - | [[Category: Chatterjee, D]] | + | [[Category: Chatterjee D]] |
| - | [[Category: Cooley, R B]] | + | [[Category: Cooley RB]] |
| - | [[Category: Mehl, R A]] | + | [[Category: Mehl RA]] |
| - | [[Category: Sondermann, H S]]
| + | [[Category: O'Toole GA]] |
| - | [[Category: Toole, G A.O]] | + | [[Category: Sondermann HS]] |
| - | [[Category: Pas-like fold]] | + | |
| - | [[Category: Signalling]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q5ZXA3_LEGPH
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chatterjee D, Cooley RB, Boyd CD, Mehl RA, O'Toole GA, Sondermann H. Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP. Elife. 2014 Sep 2;3:e03650. doi: 10.7554/eLife.03650. PMID:25182848 doi:http://dx.doi.org/10.7554/eLife.03650
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