Summary for 1K4Z
| Entry DOI | 10.2210/pdb1k4z/pdb |
| Related | 1F5I |
| Descriptor | Adenylyl Cyclase-Associated Protein (2 entities in total) |
| Functional Keywords | right-handed parallel beta-helix, intertwined dimer, actin-binding, new york sgx research center for structural genomics, nysgxrc, structural genomics, psi, protein structure initiative, membrane protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 35081.28 |
| Authors | Rozwarski, D.A.,Fedorov, A.A.,Dodatko, T.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2001-10-09, release date: 2002-03-13, Last modification date: 2024-10-30) |
| Primary citation | Dodatko, T.,Fedorov, A.A.,Grynberg, M.,Patskovsky, Y.,Rozwarski, D.A.,Jaroszewski, L.,Aronoff-Spencer, E.,Kondraskina, E.,Irving, T.,Godzik, A.,Almo, S.C. Crystal structure of the actin binding domain of the cyclase-associated protein Biochemistry, 43:10628-10641, 2004 Cited by PubMed Abstract: 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. PubMed: 15311924DOI: 10.1021/bi049071r PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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