1ryx
From Proteopedia
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'''Crystal structure of hen serum transferrin in apo- form''' | '''Crystal structure of hen serum transferrin in apo- form''' | ||
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[[Category: Dattagupta, J K.]] | [[Category: Dattagupta, J K.]] | ||
[[Category: Thakurta, P G.]] | [[Category: Thakurta, P G.]] | ||
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| - | [[Category: | + | [[Category: Hen serum transferrin]] |
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Revision as of 05:04, 3 May 2008
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 Page seeded by OCA on Sat May 3 08:04:58 2008
