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1tjf
From Proteopedia
(Difference between revisions)
(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="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | 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== |
| - | Cyclase-associated protein (CAP) is a highly conserved and widely | + | <StructureSection load='1tjf' size='340' side='right'caption='[[1tjf]], [[Resolution|resolution]] 2.21Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1tjf]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TJF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tjf OCA], [https://pdbe.org/1tjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tjf RCSB], [https://www.ebi.ac.uk/pdbsum/1tjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tjf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAP_DICDI CAP_DICDI] May have a regulatory bifunctional role. Binds G-actin and PIP2. Involved in microfilament reorganization near the plasma membrane in a PIP2-regulated manner. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tj/1tjf_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tjf ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:15558566</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1tjf" style="background-color:#fffaf0;"></div> | |
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| - | + | ||
| - | + | ==See Also== | |
| + | *[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dictyostelium discoideum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hofmann A]] | ||
| + | [[Category: Hu NJ]] | ||
| + | [[Category: Mohd Yusof A]] | ||
| + | [[Category: Wlodawer A]] | ||
Current revision
The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation
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