1tjf
From Proteopedia
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| - | [[Image:1tjf.gif|left|200px]] | + | [[Image:1tjf.gif|left|200px]] |
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| - | '''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation''' | + | {{Structure |
| + | |PDB= 1tjf |SIZE=350|CAPTION= <scene name='initialview01'>1tjf</scene>, resolution 2.21Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | ||
| + | }} | ||
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| + | '''The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TJF is a [ | + | 1TJF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJF OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15558566 15558566] |
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:19:07 2008'' |
Revision as of 12:19, 20 March 2008
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| , resolution 2.21Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CAP (Dictyostelium discoideum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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