1tfa: Difference between revisions
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|PDB= 1tfa |SIZE=350|CAPTION= <scene name='initialview01'>1tfa</scene>, resolution 1.90Å | |PDB= 1tfa |SIZE=350|CAPTION= <scene name='initialview01'>1tfa</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfa OCA], [http://www.ebi.ac.uk/pdbsum/1tfa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfa RCSB]</span> | |||
}} | }} | ||
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[[Category: Mizutani, K.]] | [[Category: Mizutani, K.]] | ||
[[Category: Yamashita, H.]] | [[Category: Yamashita, H.]] | ||
[[Category: iron binding protein]] | [[Category: iron binding protein]] | ||
[[Category: ovotransferrin]] | [[Category: ovotransferrin]] | ||
[[Category: transferrin]] | [[Category: 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 23:55:17 2008'' | ||
Revision as of 23:55, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OVOTRANSFERRIN, N-TERMINAL LOBE, APO FORM
OverviewOverview
Transferrins bind Fe3+ very tightly in a closed interdomain cleft by the coordination of four protein ligands (Asp60, Tyr92, Tyr191, and His250 in ovotransferrin N-lobe) and of a synergistic anion, physiologically bidentate CO32-. Upon Fe3+ uptake, transferrins undergo a large scale conformational transition: the apo structure with an opening of the interdomain cleft is transformed into the closed holo structure, implying initial Fe3+ binding in the open form. To solve the Fe3+-loaded, domain-opened structure, an ovotransferrin N-lobe crystal that had been grown as the apo form was soaked with Fe3+-nitrilotriacetate, and its structure was solved at 2.1 A resolution. The Fe3+-soaked form showed almost exactly the same overall open structure as the iron-free apo form. The electron density map unequivocally proved the presence of an iron atom with the coordination by the two protein ligands of Tyr92-OH and Tyr191-OH. Other Fe3+ coordination sites are occupied by a nitrilotriacetate anion, which is stabilized through the hydrogen bonds with the peptide NH groups of Ser122, Ala123, and Gly124 and a side chain group of Thr117. There is, however, no clear interaction between the nitrilotriacetate anion and the synergistic anion binding site, Arg121.
About this StructureAbout this Structure
1TFA is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe., Mizutani K, Yamashita H, Kurokawa H, Mikami B, Hirose M, J Biol Chem. 1999 Apr 9;274(15):10190-4. PMID:10187803
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