1LCF

CRYSTAL STRUCTURE OF COPPER-AND OXALATE-SUBSTITUTED HUMAN LACTOFERRIN AT 2.0 ANGSTROMS RESOLUTION

Summary for 1LCF

• Entry DOI: 10.2210/pdb1lcf/pdb
• Descriptor: LACTOFERRIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (6 entities in total)
• Functional Keywords: iron transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 76717.56

Authors

Smith, C.A.,Anderson, B.F.,Baker, H.M.,Baker, E.N. (deposition date: 1994-01-11, release date: 1994-08-31, Last modification date: 2020-07-29)

Primary citation

Smith, C.A.,Anderson, B.F.,Baker, H.M.,Baker, E.N.
Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution.
Acta Crystallogr.,Sect.D, 50:302-316, 1994

PubMed Abstract: The three-dimensional structure of human dicupric monooxalate lactoferrin, Cu(2)oxLf, has been determined to 2.0 A resolution, using X-ray diffraction data collected by diffractometry to 2.5 A resolution, and oscillation photography on a synchrotron source to 2.0 A resolution. Difference electron-density maps calculated between Cu(2)oxLf and both dicupric lactoferrin, Cu(2)Lf, and diferric lactoferrin, Fe(2)Lf, showed that the oxalate had replaced a carbonate in the C-terminal binding site, and that, relative to Cu(2)Lf, there were no significant differences in the N-terminal site. The structure was then refined crystallographically by restrained least-squares methods. The final model, in which the r.m.s. deviation in bond distances is 0.017 A, contains 5314 protein atoms (691 residues), two Cu(2+) ions, one bicarbonate ion, one oxalate ion, 325 solvent molecules and one sugar residue. The crystallographic R factor of 0.193 is for 46 134 reflections in the range 8.0 to 2.0 A resolution. The oxalate ion is coordinated to copper in a 1,2-bidentate fashion, and the added bulk of the anion results in the rearrangement of the side chains of nearby arginine and tyrosine residues. No other major alterations in the molecule can be observed, the overall protein structure being the same as that for Cu(2)Lf and Fe(2)Lf.

PubMed: 15299444
DOI: 10.1107/S0907444994000491

Experimental method

X-RAY DIFFRACTION (2 Å)