PDBsum entry 1k4z

Membrane protein

PDB id: 1k4z

Contents

Protein chains

157 a.a. *

Waters ×160

* Residue conservation analysis

PDB id:

1k4z

Name:

Membrane protein

Title:

C-terminal domain of cyclase associated protein

Structure:

Adenylyl cyclase-associated protein. Chain: a, b. Fragment: c-terminal domain. Synonym: cap. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

2.30Å R-factor: 0.207 R-free: 0.242

Authors:

D.A.Rozwarski,A.A.Fedorov,T.Dodatko,S.C.Almo,S.K.Burley,New York Sgx Research Center For Structural Genomics (Nysgxrc)

Key ref:

T.Dodatko et al. (2004). Crystal structure of the actin binding domain of the cyclase-associated protein. Biochemistry, 43, 10628-10641. PubMed id: 15311924 DOI: 10.1021/bi049071r

Date:

09-Oct-01 Release date: 13-Mar-02

Supersedes:

1f5i

Protein chains

P17555  (CAP_YEAST) -  Adenylyl cyclase-associated protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 526 a.a.

Struc: 157 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1021/bi049071r

Biochemistry 43:10628-10641 (2004)

PubMed id: 15311924

Crystal structure of the actin binding domain of the cyclase-associated protein.

T.Dodatko, A.A.Fedorov, M.Grynberg, Y.Patskovsky, D.A.Rozwarski, L.Jaroszewski, E.Aronoff-Spencer, E.Kondraskina, T.Irving, A.Godzik, S.C.Almo.

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.