1ryx: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
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|RELATEDENTRY=[[1n04|1N04]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ryx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ryx OCA], [http://www.ebi.ac.uk/pdbsum/1ryx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ryx RCSB]</span> | |||
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[[Category: hen serum transferrin]] | [[Category: hen serum transferrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:34:57 2008'' | ||
Revision as of 23:34, 30 March 2008
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| , resolution 3.50Å | |||||||
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| Related: | 1N04
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of hen serum transferrin in apo- form
OverviewOverview
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 StructureAbout this Structure
1RYX is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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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