PDBsum entry 1ak7

Actin depolymerization factor

PDB id: 1ak7

Contents

Protein chain

174 a.a. *

* Residue conservation analysis

PDB id:

1ak7

Name:

Actin depolymerization factor

Title:

Destrin, nmr, 20 structures

Structure:

Destrin. Chain: a. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Cellular_location: cytoplasm and nucleus. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

H.Hatanaka,K.Moriyama,K.Ogura,S.Ichikawa,I.Yahara,F.Inagaki

Key ref:

H.Hatanaka et al. (1996). Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell, 85, 1047-1055. PubMed id: 8674111 DOI: 10.1016/S0092-8674(00)81305-7

Date:

29-May-97 Release date: 15-Oct-97

Protein chain

P60982  (DEST_PIG) -  Destrin from Sus scrofa

Seq: 165 a.a.

Struc: 174 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/S0092-8674(00)81305-7

Cell 85:1047-1055 (1996)

PubMed id: 8674111

Tertiary structure of destrin and structural similarity between two actin-regulating protein families.

H.Hatanaka, K.Ogura, K.Moriyama, S.Ichikawa, I.Yahara, F.Inagaki.

ABSTRACT

Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes. We determined the tertiary structure of destrin by triple-resonance multidimensional nuclear magnetic resonance. In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group. Sequential dissimilarity of the actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive phosphoinositide-competitive actin binding, of pH-dependent filament severing, and of nuclear translocation with actin in response to stresses, are discussed on the basis of the tertiary structure.

Selected figure(s)

Figure 3.
Figure 3. Relationship between the Cofilin and Gelsolin Families(A) Superposition of the mean structures of destrin (black) and three members of the gelsolin family (red, gelsolin segment-1; green, villin segment-1; blue, severin segment-2). We used coordinates provided by [44], Model 1 in Protein Data Bank entry 1VIL ( [40]), and Protein Data Bank entry 1SVR ( [61]), respectively. The regions used for superposition are described in the text and also shown here in bold lines. Start and end residues of the regions are numbered.(B) Sequence alignments of destrin and gelsolin family members whose tertiary structures have been solved. Meaningful residues are colored (green, hydrophobic; red, acidic; blue, basic). Regular secondary structure elements are underlined and boxed by colors (yellow, α helix; light blue, β strand). The sequences of destrin and gelsolin segment-1 are numbered, and numbering of the latter is adjusted to the plasma-form corresponding to [44]. Regions used for the superposition in (A) are represented by dotted lines.

Figure 4.
Figure 4. Actin Binding by Destrin(A) Model of the complex of actin (green) and destrin (yellow) made from coordinates of the complex of actin and gelsolin segment-1 ([44]). Destrin is superposed on gelsolin segment-1, as shown in Figure 3A, and gelsolin segment-1 is hidden. The actin-binding helix is colored red.(B) Assumed actin-binding residues in destrin (top) and actual actin-binding residues in gelsolin segment-1 (bottom) elucidated by [44]. Destrin can be related to Figure 2 by 20° y rotation. The two molecules are oriented by the superposition described in Figure 3A. Molecular surfaces were produced using the program GRASP ( [51]) and colored according to amino acid residue type (yellow, hydrophobic; red, acidic; blue, basic; white, others) instead of usual surface electric potential.

The above figures are reprinted by permission from Cell Press: Cell (1996, 85, 1047-1055) copyright 1996.

Figures were selected by an automated process.