2PRF

THREE DIMENSIONAL SOLUTION STRUCTURE OF ACANTHAMOEBA PROFILIN I

Summary for 2PRF

• Entry DOI: 10.2210/pdb2prf/pdb
• Descriptor: PROFILIN IA (1 entity in total)
• Functional Keywords: actin-binding
• Biological source: Acanthamoeba sp.
• Total number of polymer chains: 1
• Total formula weight: 12962.45

Authors

Archer, S.J.,Vinson, V.K.,Pollard, T.D.,Lattman, E.E.,Torchia, D.A. (deposition date: 1994-01-12, release date: 1994-05-31, Last modification date: 2024-05-01)

Primary citation

Vinson, V.K.,Archer, S.J.,Lattman, E.E.,Pollard, T.D.,Torchia, D.A.
Three-dimensional solution structure of Acanthamoeba profilin-I.
J.Cell Biol., 122:1277-1283, 1993

PubMed Abstract: 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.

PubMed: 8397216
DOI: 10.1083/jcb.122.6.1277

Experimental method

SOLUTION NMR