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Structural evidence for variable oligomerization of the N‐terminal domain of cyclase‐associated protein (CAP)
Author(s) -
Yusof Adlina Mohd,
Hu NienJen,
Wlodawer Alexander,
Hofmann Andreas
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20314
Subject(s) - dictyostelium discoideum , adenylyl cyclase , dimer , chemistry , cleavage (geology) , cytokinesis , cyclase , protein structure , biochemistry , biophysics , stereochemistry , biology , signal transduction , receptor , cell division , cell , paleontology , organic chemistry , gene , fracture (geology)
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 Å 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. Proteins 2005. © 2004 Wiley‐Liss, Inc.