1KSR

THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES

Summary for 1KSR

• Entry DOI: 10.2210/pdb1ksr/pdb
• Descriptor: GELATION FACTOR (1 entity in total)
• Functional Keywords: actin binding protein, immunoglobulin, gelation factor, abp-120
• Biological source: Dictyostelium discoideum
• Total number of polymer chains: 1
• Total formula weight: 10516.43

Authors

Fucini, P.,Renner, C.,Herberhold, C.,Noegel, A.A.,Holak, T.A. (deposition date: 1997-02-07, release date: 1997-08-20, Last modification date: 2024-05-22)

Primary citation

Fucini, P.,Renner, C.,Herberhold, C.,Noegel, A.A.,Holak, T.A.
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.
Nat.Struct.Biol., 4:223-230, 1997

PubMed Abstract: The 120,000 M(r) gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are rod-shaped homodimers. Each monomer chain is comprised of an actin-binding domain and a rod domain. The rod domain of the gelation factor consists of six 100-residue repetitive segments with high internal homology. We have now determined the three-dimensional structure of segment 4 of the rod domain of the gelation factor from D. discoideum using NMR spectroscopy. The segment consists of seven beta-sheets arranged in an immunoglobulin-like (Ig) fold. This is completely different from the alpha-actinin rod domain which consists of four spectrin-like alpha-helical segments. The gelation factor is the first example of an Ig-fold found in an actin-binding protein. Two highly homologous actin-binding proteins from human with similar sequences to the gelation factor, filamin and a 280,000 M(r) actin-binding protein (ABP-280), share conserved residues that form the core of the gelation factor repetitive segment structure. Thus, the segment 4 structure should be common to this subfamily of the spectrin superfamily. The structure of segment 4 together with previously published electron microscopy data, provide an explanation for the dimerization of the whole gelation factor molecule.

PubMed: 9164464
DOI: 10.1038/nsb0397-223

Experimental method

SOLUTION NMR