The structure of a contact-dependent growth-inhibition (CDI) immunity protein fromNeisseria meningitidisMC58
| Autor: | Parker M. Johnson, Bryan Boubion, William H. Eschenfeldt, Celia W. Goulding, Gyorgy Babnigg, Lucy Stols, Andrezj Joachimiak, Christopher S. Hayes, Kemin Tan |
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| Rok vydání: | 2015 |
| Předmět: |
Amino Acid Motifs
Bacterial Toxins Molecular Sequence Data Biophysics Gene Expression Sequence alignment Plasma protein binding Neisseria meningitidis Xenopus Proteins Biology Crystallography X-Ray medicine.disease_cause Biochemistry Protein Structure Secondary Research Communications Microbiology Xenopus laevis Structural Biology Immunity Antibiosis Endoribonucleases Escherichia coli Genetics medicine Animals Homology modeling Contact Inhibition Effector Escherichia coli Proteins RNA biochemical phenomena metabolism and nutrition Condensed Matter Physics Recombinant Proteins Protein Structure Tertiary Cell biology Molecular Docking Simulation Structural Homology Protein Nucleic acid Sequence Alignment Protein Binding |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 71:702-709 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x15006585 |
| Popis: | Contact-dependent growth inhibition (CDI) is an important mechanism of intercellular competition between neighboring Gram-negative bacteria. CDI systems encode large surface-exposed CdiA effector proteins that carry a variety of C-terminal toxin domains (CdiA-CTs). All CDI+bacteria also produce CdiI immunity proteins that specifically bind to the cognate CdiA-CT and neutralize its toxin activity to prevent auto-inhibition. Here, the X-ray crystal structure of a CdiI immunity protein fromNeisseria meningitidisMC58 is presented at 1.45 Å resolution. The CdiI protein has structural homology to the Whirly family of RNA-binding proteins, but appears to lack the characteristic nucleic acid-binding motif of this family. Sequence homology suggests that the cognate CdiA-CT is related to the eukaryotic EndoU family of RNA-processing enzymes. A homology model is presented of the CdiA-CT based on the structure of the XendoU nuclease fromXenopus laevis. Molecular-docking simulations predict that the CdiA-CT toxin active site is occluded upon binding to the CdiI immunity protein. Together, these observations suggest that the immunity protein neutralizes toxin activity by preventing access to RNA substrates. |
| Databáze: | OpenAIRE |
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