1ce2
From Proteopedia
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STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN AT 2.5A RESOLUTION
Overview
The structure of buffalo lactoferrin has been determined at 303 K. The, crystals belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell, parameters a = 77.5, b = 91.0, c = 131.5 A and Z = 4. The structure has, been refined to an R factor of 0.187. The overall structure of the protein, is similar to its structure determined at 277 K in a different crystal, form. However, the lobe orientations in the two structures differ by 9.0, degrees, suggesting significant inter-lobe flexibility in this family of, proteins. The inter-lobe interactions are predominantly hydrophobic and, could act as a cushion for a change in orientation under the influence of, external conditions. On the other hand, the domain arrangements are found, to be similar in 277 and 303 K crystal structures, with orientations, differing by 1.5 and 1.0 degrees in the N and C lobes, respectively. The, results of these investigations suggest that the increase in temperature, helps in the production of better quality crystals.
About this Structure
1CE2 is a Single protein structure of sequence from Bubalus bubalis with FE and CO3 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of buffalo lactoferrin at 2.5 A resolution using crystals grown at 303 K shows different orientations of the N and C lobes., Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1805-13. PMID:10531476
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