1LFH

MOLECULAR REPLACEMENT SOLUTION OF THE STRUCTURE OF APOLACTOFERRIN, A PROTEIN DISPLAYING LARGE-SCALE CONFORMATIONAL CHANGE

Summary for 1LFH

• Entry DOI: 10.2210/pdb1lfh/pdb
• Descriptor: LACTOFERRIN, CHLORIDE ION (3 entities in total)
• Functional Keywords: iron transport
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Secreted. Isoform DeltaLf: Cytoplasm: P02788
• Total number of polymer chains: 1
• Total formula weight: 76257.66

Authors

Anderson, B.F.,Baker, E.N.,Norris, G.E. (deposition date: 1991-09-04, release date: 1993-10-31, Last modification date: 2024-10-16)

Primary citation

Norris, G.E.,Anderson, B.F.,Baker, E.N.
Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.
Acta Crystallogr.,Sect.B, 47:998-1004, 1991

PubMed Abstract: The crystal structure of an orthorhombic form of human apolactoferrin (ApoLf) has been determined from 2.8 A diffractometer data by molecular replacement methods. A variety of search models derived from the diferric lactoferrin structure (Fe2Lf) were used to obtain a consistent solution to the rotation function. An R-factor search gave the correct translational solution and the model was refined by rigid-body least-squares refinement (program CORELS). Only three of the four domains were located correctly by this procedure, however; the fourth was finally placed correctly by rotating it manually onto three strands of electron density which were recognized as part of its central beta-sheet. The final model, refined by restrained least-squares methods to an R factor of 0.214 for data in the resolution range 10.0 to 2.8 A, shows a large domain movement in the N-terminal half of the molecule (a 54 degree rotation of domain N2) and smaller domain movements elsewhere, when compared with Fe2Lf. A feature of the crystal structure is that although the ApoLf and Fe2Lf unit cells appear very similar, their crystal packing and molecular structures are quite different.

PubMed: 1772635
DOI: 10.1107/S0108768191008418

Experimental method

X-RAY DIFFRACTION (2.8 Å)