1k4z

<StructureSection load='1k4z' size='340' side='right'caption='[[1k4z]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1k4z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K4Z FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f5i|1f5i]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4z OCA], [http://pdbe.org/1k4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k4z RCSB], [http://www.ebi.ac.uk/pdbsum/1k4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k4z ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1k4z TOPSAN]</span></td></tr>

== Function ==

[[http://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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== Publication Abstract from PubMed ==

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.

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:15311924<ref>PMID:15311924</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1k4z" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Almo, S C]]

[[Category: Burley, S K]]

[[Category: Dodatko, T]]

[[Category: Fedorov, A A]]

[[Category: Structural genomic]]

[[Category: Rozwarski, D A]]

[[Category: Right-handed parallel beta-helix]]