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1tjf
From Proteopedia
(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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| - | [[Image:1tjf.gif|left|200px]]<br /><applet load="1tjf" size=" | + | [[Image:1tjf.gif|left|200px]]<br /><applet load="1tjf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tjf, resolution 2.21Å" /> | caption="1tjf, resolution 2.21Å" /> | ||
'''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation'''<br /> | '''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cyclase-associated protein (CAP) is a highly conserved and widely | + | 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== | ==About this Structure== | ||
| - | 1TJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TJF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJF OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hofmann, A.]] | [[Category: Hofmann, A.]] | ||
| - | [[Category: Hu, N | + | [[Category: Hu, N J.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: Yusof, A | + | [[Category: Yusof, A Mohd.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:10 2008'' |
Revision as of 13:14, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 15:14:10 2008
