Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator ▿†
| Autor: | Aaron M. Ginster, Katrina T. Forest, Gregory A. Worzalla, Timothy J. Cordes |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Cyclic AMP Receptor Protein Protein Conformation Virulence Factors Regulator Virulence medicine.disease_cause Microbiology DNA-binding protein Virulence factor Bacterial Proteins Structural Biology medicine Transcriptional regulation Cloning Molecular Molecular Biology biology Pseudomonas aeruginosa Pseudomonas Gene Expression Regulation Bacterial biology.organism_classification Molecular biology Mutagenesis Site-Directed Crystallization |
| Popis: | Virulence factor regulator (Vfr) enhances Pseudomonas aeruginosa pathogenicity through its role as a global transcriptional regulator. The crystal structure of Vfr shows that it is a winged-helix DNA-binding protein like its homologue cyclic AMP receptor protein (CRP). In addition to an expected primary cyclic AMP-binding site, a second ligand-binding site is nestled between the N-terminal domain and the C-terminal helix-turn-helix domain. Unlike CRP, Vfr is a symmetric dimer in the absence of DNA. Removal of seven disordered N-terminal residues of Vfr prevents the growth of P. aeruginosa . |
| Databáze: | OpenAIRE |
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