1lcf

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spinqualitylabelsall models 1lcf, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Deafness, autosomal dominant 1 OMIM:[602121]

About this Structure

1LCF is a Single protein structure of sequence from Homo sapiens with NAG, CU, CO3 and OXL as ligands. Full crystallographic information is available from OCA.

Reference

Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution., Smith CA, Anderson BF, Baker HM, Baker EN, Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):302-16. PMID:15299444

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