1PRQ
ACANTHAMOEBA CASTELLANII PROFILIN IA
Summary for 1PRQ
| Entry DOI | 10.2210/pdb1prq/pdb |
| Descriptor | PROFILIN IA (2 entities in total) |
| Functional Keywords | actin-binding protein, contractile protein |
| Biological source | Acanthamoeba castellanii |
| Cellular location | Cytoplasm, cytoskeleton: P68696 |
| Total number of polymer chains | 1 |
| Total formula weight | 12962.45 |
| Authors | Fedorov, A.A.,Pollard, T.D.,Way, M.,Lattman, E.E.,Almo, S.C. (deposition date: 1997-08-18, release date: 1997-12-24, Last modification date: 2024-05-22) |
| Primary citation | Liu, S.,Fedorov, A.A.,Pollard, T.D.,Lattman, E.E.,Almo, S.C.,Magnus, K.A. Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii. J.Struct.Biol., 123:22-29, 1998 Cited by PubMed Abstract: Profilin-I from Acanthamoeba castellanii is a 13-kDa protein that binds actin and poly-l-proline. The native protein has been crystallized in two different but closely related forms. The second form proved more amenable to three-dimensional structural determination using heavy-atom isomorphous methods to obtain crystallographic phase information. We used the second crystal structure as a test molecule in the molecular replacement procedure to determine the structure of the first crystal form of profilin-I. More residues participate in crystal lattice contacts in the first crystal form than in the second. The two crystal forms differ significantly in the C-terminal helix that interacts with actin and in the loop preceding this helix. Coordinates of some main chain atoms here differ by about 1.0 A, and side chain atoms differ by more than 2.0 A. PubMed: 9774541DOI: 10.1006/jsbi.1998.4009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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