Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5EUH

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

Summary for 5EUH
Entry DOI10.2210/pdb5euh/pdb
DescriptorPutative GGDEF domain membrane protein, 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), SULFATE ION, ... (4 entities in total)
Functional Keywordsdiguanylate cyclase, second messenger, biofilm formation, signaling, membrane protein
Biological sourcePseudomonas fluorescens (strain Pf0-1)
Total number of polymer chains4
Total formula weight79495.15
Authors
Giglio, K.M.,Cooley, R.B.,Sondermann, H. (deposition date: 2015-11-18, release date: 2015-12-30, Last modification date: 2023-09-27)
Primary citationDahlstrom, K.M.,Giglio, K.M.,Collins, A.J.,Sondermann, H.,O'Toole, G.A.
Contribution of Physical Interactions to Signaling Specificity between a Diguanylate Cyclase and Its Effector.
Mbio, 6:e01978-e01915, 2015
Cited by
PubMed Abstract: 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.
PubMed: 26670387
DOI: 10.1128/mBio.01978-15
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.989 Å)
Structure validation

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon