6PWJ
Vibrio cholerae LapD S helix-GGDEF-EAL (apo)
Summary for 6PWJ
Entry DOI | 10.2210/pdb6pwj/pdb |
Descriptor | GGDEF and EAL domain-containing protein, MAGNESIUM ION, TRIETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | biofilm formation, cell adhesion, c-di-gmp signaling, receptor, signaling protein |
Biological source | Vibrio cholerae O1 str. 2010EL-1786 |
Total number of polymer chains | 2 |
Total formula weight | 94849.07 |
Authors | Giglio, K.M.,Cooley, R.B.,Sondermann, H. (deposition date: 2019-07-23, release date: 2019-10-09, Last modification date: 2024-03-13) |
Primary citation | Kitts, G.,Giglio, K.M.,Zamorano-Sanchez, D.,Park, J.H.,Townsley, L.,Cooley, R.B.,Wucher, B.R.,Klose, K.E.,Nadell, C.D.,Yildiz, F.H.,Sondermann, H. A Conserved Regulatory Circuit Controls Large Adhesins in Vibrio cholerae. Mbio, 10:-, 2019 Cited by PubMed Abstract: The dinucleotide second messenger c-di-GMP has emerged as a central regulator of reversible cell attachment during bacterial biofilm formation. A prominent cell adhesion mechanism first identified in pseudomonads combines two c-di-GMP-mediated processes: transcription of a large adhesin and its cell surface display via posttranslational proteolytic control. Here, we characterize an orthologous c-di-GMP effector system and show that it is operational in , where it regulates two distinct classes of adhesins. Through structural analyses, we reveal a conserved autoinhibition mechanism of the c-di-GMP receptor that controls adhesin proteolysis and present a structure of a c-di-GMP-bound receptor module. We further establish functionality of the periplasmic protease controlled by the receptor against the two adhesins. Finally, transcription and functional assays identify physiological roles of both c-di-GMP-regulated adhesins in surface attachment and biofilm formation. Together, our studies highlight the conservation of a highly efficient signaling effector circuit for the control of cell surface adhesin expression and its versatility by revealing strain-specific variations., the causative agent of the diarrheal disease cholera, benefits from a sessile biofilm lifestyle that enhances survival outside the host but also contributes to host colonization and infectivity. The bacterial second messenger c-di-GMP has been identified as a central regulator of biofilm formation, including in ; however, our understanding of the pathways that contribute to this process is incomplete. Here, we define a conserved signaling system that controls the stability of large adhesion proteins at the cell surface of , which are important for cell attachment and biofilm formation. Insight into the regulatory circuit underlying biofilm formation may inform targeted strategies to interfere with a process that renders this bacterium remarkably adaptable to changing environments. PubMed: 31796544DOI: 10.1128/mBio.02822-19 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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