1k4z
From Proteopedia
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|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00673 CARP], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08603 CAP_C]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00673 CARP], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam08603 CAP_C]</span> | ||
| - | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1k4z PDBsum | + | |RELATEDENTRY=[[1f5i|1F5I]] |
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1k4z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4z RCSB]</span> | ||
}} | }} | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:43:31 2008'' |
Revision as of 18:43, 30 March 2008
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| , resolution 2.30Å | |||||||
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| Domains: | CARP, CAP_C | ||||||
| Related: | 1F5I
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
C-terminal Domain of Cyclase Associated Protein
Overview
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.
About this Structure
1K4Z is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 1F5I. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 21:43:31 2008
Categories: Saccharomyces cerevisiae | Single protein | Almo, S C. | Burley, S K. | Dodatko, T. | Fedorov, A A. | NYSGXRC, New York Structural GenomiX Research Consortium. | Rozwarski, D A. | Actin-binding | Intertwined dimer | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Right-handed parallel beta-helix | Structural genomic
