1TJF

The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation

Summary for 1TJF

• Entry DOI: 10.2210/pdb1tjf/pdb
• Descriptor: Adenylyl cyclase-associated protein, SULFATE ION (3 entities in total)
• Functional Keywords: membrane protein, protein binding
• Biological source: Dictyostelium discoideum
• Cellular location: Cell membrane; Peripheral membrane protein: P54654
• Total number of polymer chains: 2
• Total formula weight: 41498.42

Authors

Mohd Yusof, A.,Hu, N.J.,Wlodawer, A.,Hofmann, A. (deposition date: 2004-06-04, release date: 2005-02-01, Last modification date: 2023-08-23)

Primary citation

Mohd Yusof, A.,Hu, N.J.,Wlodawer, A.,Hofmann, A.
Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).
Proteins, 58:255-262, 2005

PubMed Abstract: Cyclase-associated protein (CAP) is a highly conserved and widely distributed protein that links the nutritional response signaling to cytoskeleton remodeling. In yeast, CAP is a component of the adenylyl cyclase complex and helps to activate the Ras-mediated catalytic cycle of the cyclase. While the N-terminal domain of CAP (N-CAP) provides a binding site for adenylyl cyclase, the C-terminal domain (C-CAP) possesses actin binding activity. Our attempts to crystallize full-length recombinant CAP from Dictyostelium discoideum resulted in growth of orthorhombic crystals containing only the N-terminal domain (residues 42-227) due to auto-proteolytic cleavage. The structure was solved by molecular replacement with data at 2.2 A resolution. The present crystal structure allows the characterization of a head-to-tail N-CAP dimer in the asymmetric unit and a crystallographic side-to-side dimer. Comparison with previously published structures of N-CAP reveals variable modes of dimerization of this domain, but the presence of a common interface for the side-to-side dimer.

PubMed: 15558566
DOI: 10.1002/prot.20314

Experimental method

X-RAY DIFFRACTION (2.21 Å)