1tjf
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(New page: 200px<br /><applet load="1tjf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tjf, resolution 2.21Å" /> '''The crystal structur...)
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Revision as of 01:12, 21 November 2007
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The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation
Overview
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.
About this Structure
1TJF is a Single protein structure of sequence from Dictyostelium discoideum with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Structural evidence for variable oligomerization of the N-terminal domain of cyclase-associated protein (CAP)., Yusof AM, Hu NJ, Wlodawer A, Hofmann A, Proteins. 2005 Feb 1;58(2):255-62. PMID:15558566
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