1pgu
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1pgu.gif|left|200px]] | [[Image:1pgu.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1pgu", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1pgu| PDB=1pgu | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM''' | '''YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM''' | ||
| Line 28: | Line 25: | ||
[[Category: Voegtli, W C.]] | [[Category: Voegtli, W C.]] | ||
[[Category: Wilson, D K.]] | [[Category: Wilson, D K.]] | ||
| - | [[Category: | + | [[Category: Seven-bladed beta-propeller]] |
| - | [[Category: | + | [[Category: Wd repeat]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:04:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:04, 3 May 2008
YEAST ACTIN INTERACTING PROTEIN 1 (AIP1), Se-Met PROTEIN, MONOCLINIC CRYSTAL FORM
Overview
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.
About this Structure
1PGU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization., Voegtli WC, Madrona AY, Wilson DK, J Biol Chem. 2003 Sep 5;278(36):34373-9. Epub 2003 Jun 14. PMID:12807914 Page seeded by OCA on Sat May 3 05:04:16 2008
