Structure of the TPR domain of p67phox in complex with Rac.GTP

Mol Cell. 2000 Oct;6(4):899-907. doi: 10.1016/s1097-2765(05)00091-2.

Abstract

p67phox is an essential part of the NADPH oxidase, a multiprotein enzyme complex that produces superoxide ions in response to microbial infection. Binding of the small GTPase Rac to p67phox is a key step in the assembly of the active enzyme complex. The structure of Rac.GTP bound to the N-terminal TPR (tetratricopeptide repeat) domain of p67phox reveals a novel mode of Rho family/effector interaction and explains the basis of GTPase specificity. Complex formation is largely mediated by an insertion between two TPR motifs, suggesting an unsuspected versatility of TPR domains in target recognition and in their more general role as scaffolds for the assembly of multiprotein complexes.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Calorimetry
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • NADPH Dehydrogenase / chemistry
  • NADPH Dehydrogenase / metabolism
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism*
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Repetitive Sequences, Amino Acid
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Thermodynamics
  • rac GTP-Binding Proteins / chemistry*
  • rac GTP-Binding Proteins / metabolism*

Substances

  • Phosphoproteins
  • Recombinant Proteins
  • neutrophil cytosol factor 67K
  • Guanosine Triphosphate
  • NADPH Dehydrogenase
  • rac2 GTP-binding protein
  • rac GTP-Binding Proteins

Associated data

  • PDB/1E96
  • PDB/1MH1