1ryx: Difference between revisions
New page: left|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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[[Image:1ryx.jpg|left|200px]]<br /><applet load="1ryx" size=" | [[Image:1ryx.jpg|left|200px]]<br /><applet load="1ryx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ryx, resolution 3.50Å" /> | caption="1ryx, resolution 3.50Å" /> | ||
'''Crystal structure of hen serum transferrin in apo- form'''<br /> | '''Crystal structure of hen serum transferrin in apo- form'''<br /> | ||
==Overview== | ==Overview== | ||
The iron binding and release of serum transferrin are pH-dependent and | 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== | ==About this Structure== | ||
1RYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http:// | 1RYX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RYX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Choudhury, D.]] | [[Category: Choudhury, D.]] | ||
[[Category: Dasgupta, R.]] | [[Category: Dasgupta, R.]] | ||
[[Category: Dattagupta, J | [[Category: Dattagupta, J K.]] | ||
[[Category: Thakurta, P | [[Category: Thakurta, P G.]] | ||
[[Category: apo- form]] | [[Category: apo- form]] | ||
[[Category: domain orientation]] | [[Category: domain orientation]] | ||
[[Category: hen serum transferrin]] | [[Category: hen serum transferrin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:02 2008'' | ||
Revision as of 12:56, 21 February 2008
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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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