1tjf: Difference between revisions
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New page: left|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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== | ==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> | |||
==See Also== | |||
*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hofmann | [[Category: Hofmann A]] | ||
[[Category: Hu | [[Category: Hu NJ]] | ||
[[Category: | [[Category: Mohd Yusof A]] | ||
[[Category: | [[Category: Wlodawer A]] | ||
Latest revision as of 06:30, 23 August 2023
The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation
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