1ACF
ACANTHAMOEBA CASTELLANII PROFILIN IB
Summary for 1ACF
| Entry DOI | 10.2210/pdb1acf/pdb |
| Descriptor | PROFILIN I (2 entities in total) |
| Functional Keywords | protein binding, profilin, actin-binding protein, contractile protein |
| Biological source | Acanthamoeba castellanii |
| Total number of polymer chains | 1 |
| Total formula weight | 12849.33 |
| Authors | Fedorov, A.A.,Magnus, K.A.,Graupe, M.H.,Lattman, E.E.,Pollard, T.D.,Almo, S.C. (deposition date: 1994-07-29, release date: 1994-08-31, Last modification date: 2024-02-07) |
| Primary citation | Fedorov, A.A.,Magnus, K.A.,Graupe, M.H.,Lattman, E.E.,Pollard, T.D.,Almo, S.C. X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proc.Natl.Acad.Sci.USA, 91:8636-8640, 1994 Cited by PubMed Abstract: We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin. PubMed: 8078936DOI: 10.1073/pnas.91.18.8636 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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