1tjf
From Proteopedia
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|PDB= 1tjf |SIZE=350|CAPTION= <scene name='initialview01'>1tjf</scene>, resolution 2.21Å | |PDB= 1tjf |SIZE=350|CAPTION= <scene name='initialview01'>1tjf</scene>, resolution 2.21Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | |GENE= CAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tjf OCA], [http://www.ebi.ac.uk/pdbsum/1tjf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tjf RCSB]</span> | ||
}} | }} | ||
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[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: Yusof, A Mohd.]] | [[Category: Yusof, A Mohd.]] | ||
| - | [[Category: SO4]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:51 2008'' |
Revision as of 20:56, 30 March 2008
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| , resolution 2.21Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CAP (Dictyostelium discoideum) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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