1ryx
From Proteopedia
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| - | [[Image:1ryx.jpg|left|200px]] | + | [[Image:1ryx.jpg|left|200px]] |
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| - | '''Crystal structure of hen serum transferrin in apo- form''' | + | {{Structure |
| + | |PDB= 1ryx |SIZE=350|CAPTION= <scene name='initialview01'>1ryx</scene>, resolution 3.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of hen serum transferrin in apo- form''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RYX is a [ | + | 1RYX is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15044101 15044101] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hen serum transferrin]] | [[Category: hen serum transferrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:58:11 2008'' |
Revision as of 11:58, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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