Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator

Journal Article · Fri Sep 07 00:00:00 EDT 2012 · Journal of Bacteriology

DOI:https://doi.org/10.1128/JB.00666-10· OSTI ID:1050738

Cordes, Timothy J; Worzalla, Gregory A; Ginster, Aaron M; Forest, Katrina T ^[1]

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1. UW

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 prvents the growth of P. aeruginosa.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: OTHERUNIVERSITYNIHOTHER U.S. GOVERNMENT
• OSTI ID: 1050738
• Journal Information: Journal of Bacteriology, Vol. 193, Issue 16; ISSN 0021-9193
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
AMP
CRYSTAL STRUCTURE
DIMERS
DNA
GROWTH
PROTEINS
PSEUDOMONAS
RECEPTORS
REMOVAL
RESIDUES
VIRULENCE