The Crystal Structure of the Phosphorylation Domain in PhoP Reveals a Functional Tandem Association Mediated by an Asymmetric Interface

Lignende værker

• Residue R113 Is Essential for PhoP Dimerization and Function: a Residue Buried in the Asymmetric PhoP Dimer Interface Determined in the PhoPN Three-Dimensional Crystal Structure
  af: Chen, Yinghua, et al.
  Udgivet: (2003)
• Residues Required for Bacillus subtilis PhoP DNA Binding or RNA Polymerase Interaction: Alanine Scanning of PhoP Effector Domain Transactivation Loop and α Helix 3
  af: Chen, Yinghua, et al.
  Udgivet: (2004)
• Bacillus subtilis Phosphorylated PhoP: Direct Activation of the Eσ(A)- and Repression of the Eσ(E)-Responsive phoB-P(S+V) Promoters during Pho Response
  af: Abdel-Fattah, Wael R., et al.
  Udgivet: (2005)
• PhoP-PhoP Interaction at Adjacent PhoP Binding Sites Is Influenced by Protein Phosphorylation
  af: Sinha, Akesh, et al.
  Udgivet: (2008)
• Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter.
  af: Liu, W, et al.
  Udgivet: (1997)