Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).
Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP).
复制标题
环化酶相关蛋白 (CAP) N 末端结构域可变寡聚化的结构证据。
DOI：
10.1002/prot.20314
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发表时间：
2005
期刊：
影响因子：
2.9
通讯作者：
Hofmann,Andreas
中科院分区：
文献类型：
--
作者：
Yusof,AdlinaMohd;Hu,Nien-Jen;Wlodawer,Alexander;Hofmann,Andreas
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 fromDictyostelium discoideumresulted 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.
