5euh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 5euh is ON HOLD Authors: Giglio, K.M., Cooley, R.B., Sondermann, H. Description: Crystal structure of the c-di-GMP-bound GGDEF domain of P. fluores...)
Current revision (08:25, 12 July 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5euh is ON HOLD
+
==Crystal structure of the c-di-GMP-bound GGDEF domain of P. fluorescens GcbC==
 +
<StructureSection load='5euh' size='340' side='right'caption='[[5euh]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5euh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens_Pf0-1 Pseudomonas fluorescens Pf0-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EUH 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]] 2.989&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5euh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5euh OCA], [https://pdbe.org/5euh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5euh RCSB], [https://www.ebi.ac.uk/pdbsum/5euh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5euh ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q3K751_PSEPF Q3K751_PSEPF]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Cyclic diguanylate (c-di-GMP) is a bacterial second messenger that controls multiple cellular processes. c-di-GMP networks have up to dozens of diguanylate cyclases (DGCs) that synthesize c-di-GMP along with many c-di-GMP-responsive target proteins that can bind and respond to this signal. For such networks to have order, a mechanism(s) likely exists that allow DGCs to specifically signal their targets, and it has been suggested that physical interactions might provide such specificity. Our results show a DGC from Pseudomonas fluorescens physically interacting with its target protein at a conserved interface, and this interface can be predictive of DGC-target protein interactions. Furthermore, we demonstrate that physical interaction is necessary for the DGC to maximally signal its target. If such "local signaling" is a theme for even a fraction of the DGCs used by bacteria, it becomes possible to posit a model whereby physical interaction allows a DGC to directly signal its target protein, which in turn may help curtail undesired cross talk with other members of the network. IMPORTANCE: An important question in microbiology is how bacteria make decisions using a signaling network made up of proteins that make, break, and bind the second messenger c-di-GMP, which is responsible for controlling many cellular behaviors. Previous work has shown that a given DGC enzyme will signal for specific cellular outputs, despite making the same diffusible molecule as its sibling DGCs in the unpartitioned space of the bacterial cell. Understanding how one DGC differentiates its output from the dozens of other such enzymes in the cell is synonymous with understanding a large component of the bacterial decision-making machinery. We present evidence for a helix on a DGC used to physically associate with its target protein, which is necessary to achieve maximal signaling.
-
Authors: Giglio, K.M., Cooley, R.B., Sondermann, H.
+
Contribution of Physical Interactions to Signaling Specificity between a Diguanylate Cyclase and Its Effector.,Dahlstrom KM, Giglio KM, Collins AJ, Sondermann H, O'Toole GA MBio. 2015 Dec 15;6(6). pii: e01978-15. doi: 10.1128/mBio.01978-15. PMID:26670387<ref>PMID:26670387</ref>
-
Description: Crystal structure of the c-di-GMP-bound GGDEF domain of P. fluorescens GcbC
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Giglio, K.M]]
+
<div class="pdbe-citations 5euh" style="background-color:#fffaf0;"></div>
-
[[Category: Cooley, R.B]]
+
== References ==
-
[[Category: Sondermann, H]]
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Pseudomonas fluorescens Pf0-1]]
 +
[[Category: Cooley RB]]
 +
[[Category: Giglio KM]]
 +
[[Category: Sondermann H]]

Current revision

Crystal structure of the c-di-GMP-bound GGDEF domain of P. fluorescens GcbC

PDB ID 5euh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools