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1k4z

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(New page: 200px<br /><applet load="1k4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k4z, resolution 2.30&Aring;" /> '''C-terminal Domain of...)
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[[Image:1k4z.gif|left|200px]]<br /><applet load="1k4z" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1k4z, resolution 2.30&Aring;" />
 
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'''C-terminal Domain of Cyclase Associated Protein'''<br />
 
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==Overview==
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==C-terminal Domain of Cyclase Associated Protein==
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Cyclase-associated protein (CAP or Srv2p) is a modular actin monomer, binding protein that directly regulates filament dynamics and has been, implicated in a number of complex developmental and morphological, processes, including mRNA localization and the establishment of cell, polarity. The crystal structure of the C-terminal dimerization and actin, monomer binding domain (C-CAP) reveals a highly unusual dimer, composed of, monomers possessing six coils of right-handed beta-helix flanked by, antiparallel beta-strands. Domain swapping, involving the last two strands, of each monomer, results in the formation of an extended dimer with an, extensive interface. This structural and biochemical characterization, provides new insights into the organization and potential mechanistic, properties of the multiprotein assemblies that integrate dynamic actin, processes into the overall physiology of the cell. An unanticipated, finding is that the unique tertiary structure of the C-CAP monomer, provides a structural model for a wide range of molecules, including RP2, and cofactor C, proteins involved in X-linked retinitis pigmentosa and, tubulin maturation, respectively, as well as several uncharacterized, proteins that exhibit very diverse domain organizations. Thus, the unusual, right-handed beta-helical fold present in C-CAP appears to support a wide, range of biological functions.
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<StructureSection load='1k4z' size='340' side='right'caption='[[1k4z]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1k4z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1f5i 1f5i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K4Z FirstGlance]. <br>
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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]] 2.3&#8491;</td></tr>
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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=1k4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4z OCA], [https://pdbe.org/1k4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k4z RCSB], [https://www.ebi.ac.uk/pdbsum/1k4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4z ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1k4z TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAP_YEAST CAP_YEAST] The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control.
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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/k4/1k4z_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=1k4z ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1K4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure superseeds the now removed PDB entry 1F5I. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K4Z OCA].
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the actin binding domain of the cyclase-associated protein., Dodatko T, Fedorov AA, Grynberg M, Patskovsky Y, Rozwarski DA, Jaroszewski L, Aronoff-Spencer E, Kondraskina E, Irving T, Godzik A, Almo SC, Biochemistry. 2004 Aug 24;43(33):10628-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15311924 15311924]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Almo SC]]
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[[Category: Almo, S.C.]]
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[[Category: Burley SK]]
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[[Category: Burley, S.K.]]
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[[Category: Dodatko T]]
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[[Category: Dodatko, T.]]
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[[Category: Fedorov AA]]
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[[Category: Fedorov, A.A.]]
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[[Category: Rozwarski DA]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: Rozwarski, D.A.]]
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[[Category: actin-binding]]
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[[Category: intertwined dimer]]
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[[Category: new york structural genomix research consortium]]
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[[Category: nysgxrc]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: right-handed parallel beta-helix]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:52:03 2007''
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Current revision

C-terminal Domain of Cyclase Associated Protein

PDB ID 1k4z

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