PDBsum entry 1pgu

Protein binding

PDB id: 1pgu

Contents

Protein chains

606 a.a. *

Metals

_ZN ×2

Waters ×474

* Residue conservation analysis

PDB id:

1pgu

Name:

Protein binding

Title:

Yeast actin interacting protein 1 (aip1), se-met protein, monoclinic crystal form

Structure:

Actin interacting protein 1. Chain: a, b. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: aip1 or ymr092c or ym9582.17c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.202 R-free: 0.257

Authors:

W.C.Voegtli,A.Y.Madrona,D.K.Wilson

Key ref:

W.C.Voegtli et al. (2003). The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization. J Biol Chem, 278, 34373-34379. PubMed id: 12807914 DOI: 10.1074/jbc.M302773200

Date:

28-May-03 Release date: 15-Jul-03

Protein chains

P46680  (AIP1_YEAST) -  Actin-interacting protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 615 a.a.

Struc: 606 a.a.*

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

DOI no: 10.1074/jbc.M302773200

J Biol Chem 278:34373-34379 (2003)

PubMed id: 12807914

The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization.

W.C.Voegtli, A.Y.Madrona, D.K.Wilson.

ABSTRACT

Actin-interacting protein 1 (Aip1p) is a 67-kDa WD repeat protein known to regulate the depolymerization of actin filaments by cofilin and is conserved in organisms ranging from yeast to mammals. The crystal structure of Aip1p from Saccharomyces cerevisiae was determined to a 2.3-A resolution and a final crystallographic R-factor of 0.204. The structure reveals that the overall fold is formed by two connected seven-bladed beta-propellers and has important implications for the structure of Aip1 from other organisms and WD repeat-containing proteins in general. These results were unexpected because a maximum of 10 WD repeats had been reported in the literature for this protein using sequence data. The surfaces of the beta-propellers formed by the D-A and B-C loops are positioned adjacent to one another, giving Aip1p a shape that resembles an open "clamshell." The mapping of conserved residues to the structure of Aip1p reveals dense patches of conserved residues on the surface of one beta-propeller and at the interface of the two beta-propellers. These two patches of conserved residues suggest a potential binding site for F-actin on Aip1p and that the orientation of the beta-propellers with respect to one another plays a role in binding an actin-cofilin complex. In addition, the conserved interface between the domains is mediated by a number of interactions that appear to impart rigidity between the two domains of Aip1p and may make a large substrate-induced conformational change difficult.

Selected figure(s)

Figure 2.
FIG. 2. Stereoview of 2F[o] - F[c] electron density map contoured at 1.4 for residues 336-340, 350-354, and Trp-362 which confer rigidity at the -propeller interface.

Figure 3.
FIG. 3. Surface representations of Aip1p. A, Aip1p colored according to electrostatic potential: red, -10 kT; white, 0 kT; and blue, +10 kT. The molecule is in the same orientation as in Fig. 1A. B, Aip1p colored according to sequence conservation as defined under "Results." Regions of the molecular surface formed by conserved residues are colored purple. Orientation is the same as in A. C and D, Aip1p colored in the same manner as in A and B, respectively. The molecule is rotated 180° on the y axis relative to its orientation in A and B.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 34373-34379) copyright 2003.

Figures were selected by an automated process.