Three-Dimensional Solution Structure of Acanthamoeba Profilin-I

We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2 and COOH-terminal helices on one fac...

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Bibliographic Details
Published in:The Journal of cell biology 1993-09, Vol.122 (6), p.1277-1283
Main Authors: Vinson, Valda K., Archer, Sharon J., Lattman, Eaton E., Pollard, Thomas D., Torchia, Dennis A.
Format: Article
Language:English
Subjects:
Acanthamoeba
Acanthamoeba - chemistry
Acanthamoeba - metabolism
Actins
Actins - metabolism
Amino Acid Sequence
Amino acids
Animals
Atoms
Biochemistry
Biological and medical sciences
Cell biology
Cellular biology
Contractile Proteins
Diverse techniques
Fundamental and applied biological sciences. Psychology
Image Processing, Computer-Assisted
Isomerism
Magnetic Resonance Spectroscopy
Microfilament Proteins - chemistry
Molecular and cellular biology
Molecular Sequence Data
Molecules
Nuclear magnetic resonance
Nuclear structure
Phosphatidylinositol Phosphates
Phosphatidylinositols - metabolism
Profilins
Proteins
Scientific imaging
Solutions
Spectroscopy
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Summary:We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2 and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.122.6.1277