X-Ray Structures of Isoforms of the Actin-Binding Protein Profilin that Differ in their Affinity for Phosphatidylinositol Phosphates

We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 oversetcirc 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 electr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-08, Vol.91 (18), p.8636-8640
Main Authors: Fedorov, Alexander A., Magnus, Karen A., Graupe, Menachem H., Lattman, Eaton E., Pollard, Thomas D., Almo, Steven C.
Format: Article
Language:English
Subjects:
Acanthamoeba
Acanthamoeba - chemistry
Actins
Amoeba
Animals
Binding sites
Biochemistry
Contractile Proteins
Crystal structure
Crystallography, X-Ray
Electrical phases
Electrostatics
Microfilament Proteins - chemistry
Microfilament Proteins - metabolism
Models, Molecular
Molecules
Phosphatidylinositol Phosphates - metabolism
Profilins
Protein isoforms
Protein Structure, Tertiary
Proteins
Protozoan Proteins - chemistry
Protozoan Proteins - metabolism
X-rays
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Summary:We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 oversetcirc 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 electro-static 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.18.8636