5EUH
Crystal structure of the c-di-GMP-bound GGDEF domain of P. fluorescens GcbC
Summary for 5EUH
| Entry DOI | 10.2210/pdb5euh/pdb |
| Descriptor | Putative 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 Keywords | diguanylate cyclase, second messenger, biofilm formation, signaling, membrane protein |
| Biological source | Pseudomonas fluorescens (strain Pf0-1) |
| Total number of polymer chains | 4 |
| Total formula weight | 79495.15 |
| 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 citation | Dahlstrom, 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: 26670387DOI: 10.1128/mBio.01978-15 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.989 Å) |
Structure validation
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