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1tjf

From Proteopedia

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{{Seed}}
 
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[[Image:1tjf.png|left|200px]]
 
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==The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation==
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The line below this paragraph, containing "STRUCTURE_1tjf", creates the "Structure Box" on the page.
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<StructureSection load='1tjf' size='340' side='right'caption='[[1tjf]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<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>
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{{STRUCTURE_1tjf| PDB=1tjf | SCENE= }}
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tj/1tjf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tjf" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15558566}}, adds the Publication Abstract to the page
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15558566 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15558566}}
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__TOC__
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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hofmann, A.]]
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[[Category: Hofmann A]]
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[[Category: Hu, N J.]]
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[[Category: Hu NJ]]
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[[Category: Wlodawer, A.]]
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[[Category: Mohd Yusof A]]
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[[Category: Yusof, A Mohd.]]
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[[Category: Wlodawer A]]
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[[Category: Membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:50:05 2008''
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Current revision

The crystal structure of the N-terminal domain of CAP indicates variable oligomerisation

PDB ID 1tjf

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