Structure of buffalo lactoferrin at 2.5 Åresolution using crystals grown at 303 K shows different orientations of the N and C lobes

Karthikeyan, S. ; Paramasivam, M. ; Yadav, S. ; Srinivasan, A. ; Singh, T. P. (1999) Structure of buffalo lactoferrin at 2.5 Åresolution using crystals grown at 303 K shows different orientations of the N and C lobes Acta Crystallographica Section D, D55 (11). pp. 1805-1813. ISSN 0907-4449

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Official URL: http://scripts.iucr.org/cgi-bin/paper?SE0289

Related URL: http://dx.doi.org/10.1107/S0907444999010951

Abstract

The structure of buffalo lactoferrin has been determined at 303 K. The crystals belong to orthorhombic space group P212121, with unit-cell parameters a = 77.5, b = 91.0, c = 131.5 Å 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°, 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° 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.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:Conformation; Lactoferrins; Transferrins
ID Code:49103
Deposited On:18 Jul 2011 13:55
Last Modified:18 Jul 2011 13:55

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