4U64
Structure of the periplasmic output domain of the Legionella pneumophila LapD ortholog CdgS9 in the apo state
Summary for 4U64
| Entry DOI | 10.2210/pdb4u64/pdb |
| Related | 4U65 |
| Descriptor | Two component histidine kinase, GGDEF domain protein/EAL domain protein (2 entities in total) |
| Functional Keywords | signalling, pas-like fold, transferase |
| Biological source | Legionella pneumophila subsp. pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 15118.33 |
| Authors | Chatterjee, D.,Cooley, R.B.,Boyd, C.D.,Mehl, R.A.,O'Toole, G.A.,Sondermann, H.S. (deposition date: 2014-07-27, release date: 2014-08-13, Last modification date: 2024-10-23) |
| Primary citation | Chatterjee, D.,Cooley, R.B.,Boyd, C.D.,Mehl, R.A.,O'Toole, G.A.,Sondermann, H. Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP. Elife, 3:e03650-e03650, 2014 Cited by PubMed Abstract: 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. PubMed: 25182848DOI: 10.7554/eLife.03650 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.141 Å) |
Structure validation
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