2BTF
THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN
Summary for 2BTF
Entry DOI | 10.2210/pdb2btf/pdb |
Descriptor | BETA-ACTIN, PROFILIN, STRONTIUM ION, ... (4 entities in total) |
Functional Keywords | acetylation and actin-binding |
Biological source | Bos taurus (cattle) More |
Cellular location | Cytoplasm, cytoskeleton: P60712 P02584 |
Total number of polymer chains | 2 |
Total formula weight | 57253.51 |
Authors | Schutt, C.E.,Myslik, J.C.,Rozycki, M.D.,Goonesekere, N.C.W. (deposition date: 1994-01-18, release date: 1994-06-22, Last modification date: 2025-03-26) |
Primary citation | Schutt, C.E.,Myslik, J.C.,Rozycki, M.D.,Goonesekere, N.C.,Lindberg, U. The structure of crystalline profilin-beta-actin. Nature, 365:810-816, 1993 Cited by PubMed Abstract: The three-dimensional structure of bovine profilin-beta-actin has been solved to 2.55 A resolution by X-ray crystallography. There are several significant local changes in the structure of beta-actin compared with alpha-actin as well as an overall 5 degrees rotation between its two major domains. Actin molecules in the crystal are organized into ribbons through intermolecular contacts like those found in oligomeric protein assemblies. Profilin forms two extensive contacts with the actin ribbon, one of which appears to correspond to the solution contact in vitro. PubMed: 8413665DOI: 10.1038/365810a0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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