1RYX

Crystal structure of hen serum transferrin in apo- form

Summary for 1RYX

• Entry DOI: 10.2210/pdb1ryx/pdb
• Related: 1N04
• Descriptor: Ovotransferrin (1 entity in total)
• Functional Keywords: hen serum transferrin, apo- form, domain orientation, metal transport
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 75929.01

Authors

Dattagupta, J.K.,Thakurta, P.G.,Choudhury, D.,Dasgupta, R. (deposition date: 2003-12-23, release date: 2004-07-13, Last modification date: 2024-11-20)

Primary citation

Thakurta, P.G.,Choudhury, D.,Dasgupta, R.,Dattagupta, J.K.
Tertiary structural changes associated with iron binding and release in hen serum transferrin: a crystallographic and spectroscopic study
Biochem.Biophys.Res.Commun., 316:1124-1131, 2004

PubMed Abstract: 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.

PubMed: 15044101
DOI: 10.1016/j.bbrc.2004.02.165

Experimental method

X-RAY DIFFRACTION (3.5 Å)