This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4u64

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:04, 22 March 2023

Structure of the periplasmic output domain of the Legionella pneumophila LapD ortholog CdgS9 in the apo state

Structural highlights

4u64 is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. Philadelphia 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u64"

@@ Line 3: / Line 3: @@
 <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 [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>
+== Function ==
+[https://www.uniprot.org/uniprot/Q5ZXA3_LEGPH Q5ZXA3_LEGPH]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[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]]

4u64

From Proteopedia

Revision as of 08:04, 22 March 2023

Structure of the periplasmic output domain of the Legionella pneumophila LapD ortholog CdgS9 in the apo state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox