1E96

Structure of the Rac/p67phox complex

Summary for 1E96

• Entry DOI: 10.2210/pdb1e96/pdb
• Related: 1A17 1MH1
• NMR Information: BMRB: 5511
• Descriptor: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1, NEUTROPHIL CYTOSOL FACTOR 2 (NCF-2) TPR DOMAIN, RESIDUES 1-203, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: signaling protein, signalling complex, gtpase, nadph oxidase, protein-protein complex, tpr motif
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 2
• Total formula weight: 45467.02

Authors

Lapouge, K.,Smith, S.J.M.,Walker, P.A.,Gamblin, S.J.,Smerdon, S.J.,Rittinger, K. (deposition date: 2000-10-10, release date: 2000-11-17, Last modification date: 2023-12-13)

Primary citation

Lapouge, K.,Smith, S.J.,Walker, P.A.,Gamblin, S.J.,Smerdon, S.J.,Rittinger, K.
Structure of the TPR domain of p67phox in complex with Rac.GTP.
Mol.Cell, 6:899-907, 2000

PubMed 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.

PubMed: 11090627
DOI: 10.1016/s1097-2765(05)00091-2

Experimental method

X-RAY DIFFRACTION (2.4 Å)