1ryx
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(New page: 200px<br /><applet load="1ryx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryx, resolution 3.50Å" /> '''Crystal structure of...)
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Revision as of 23:51, 20 November 2007
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Crystal structure of hen serum transferrin in apo- form
Overview
The iron binding and release of serum transferrin are pH-dependent and, accompanied by a conformational change between the iron-bound (holo-) and, iron-free (apo-) forms. We have determined the crystal structure of, apo-hen serum transferrin (hAST) at 3.5A resolution, which is the first, reported structure to date of any full molecule of an apo-serum, transferrin and studied its pH-dependent iron release by UV-vis absorption, and near UV-CD spectroscopy. The crystal structure of hAST shows that both, the lobes adopt an open conformation and the relative orientations of the, domains are different from those of apo-human serum transferrin and human, apolactoferrin but similar to that of hen apo-ovotransferrin., Spectroscopic analysis reveals that in hen serum transferrin, release of, the first iron starts at a pH approximately 6.5 and continues over a broad, pH range (6.5-5.2). The complete release of the iron, however, occurs at, pH approximately 4.0. The near UV-CD spectra show alterations in the, microenvironment of the aromatic residues surrounding the iron-binding, sites.
About this Structure
1RYX is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study., Thakurta PG, Choudhury D, Dasgupta R, Dattagupta JK, Biochem Biophys Res Commun. 2004 Apr 16;316(4):1124-31. PMID:15044101
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