High-resolution crystal structure of the Borreliella burgdorferi PlzA protein in complex with c-di-GMP: new insights into the interaction of c-di-GMP with the novel xPilZ domain
| Autor: | Richard T. Marconi, Christopher Davies, Jerilyn R. Izac, Dhara T Patel, Edward J A Schuler, Avinash Singh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Microbiology (medical)
Models Molecular Stereochemistry Structural similarity Bacterial Proteins Protein Domains PlzA Borrelia Immunology and Allergy borreliella Binding site Receptor Cyclic GMP AcademicSubjects/SCI01150 General Immunology and Microbiology biology borrelia Chemistry PilZ General Medicine c-di-GMP biology.organism_classification Infectious Diseases Förster resonance energy transfer Borrelia burgdorferi biology.protein Diguanylate cyclase xPilZ Borrelia hermsii Crystallization Linker AcademicSubjects/MED00690 Research Article |
| Zdroj: | Pathogens and Disease |
| ISSN: | 2049-632X |
| Popis: | In the tick-borne pathogens, Borreliella burgdorferi and Borrelia hermsii, c-di-GMP is produced by a single diguanylate cyclase (Rrp1). In these pathogens, the Plz proteins (PlzA, B and C) are the only c-di-GMP receptors identified to date and PlzA is the sole c-di-GMP receptor found in all Borreliella isolates. Bioinformatic analyses suggest that PlzA has a unique PilZN3-PilZ architecture with the relatively uncommon xPilZ domain. Here, we present the crystal structure of PlzA in complex with c-di-GMP (1.6 Å resolution). This is the first structure of a xPilz domain in complex with c-di-GMP to be determined. PlzA has a two-domain structure, where each domain comprises topologically equivalent PilZ domains with minimal sequence identity but remarkable structural similarity. The c-di-GMP binding site is formed by the linker connecting the two domains. While the structure of apo PlzA could not be determined, previous fluorescence resonance energy transfer data suggest that apo and holo forms of the protein are structurally distinct. The information obtained from this study will facilitate ongoing efforts to identify the molecular mechanisms of PlzA-mediated regulation in ticks and mammals. Here, the authors present a high-resolution structure of the Borreliella burgdorferi PlzA protein complexed with c-di-GMP. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|