1tfa
From Proteopedia
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| - | [[Image:1tfa.gif|left|200px]] | + | [[Image:1tfa.gif|left|200px]] |
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| - | '''OVOTRANSFERRIN, N-TERMINAL LOBE, APO FORM''' | + | {{Structure |
| + | |PDB= 1tfa |SIZE=350|CAPTION= <scene name='initialview01'>1tfa</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''OVOTRANSFERRIN, N-TERMINAL LOBE, APO FORM''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TFA is a [ | + | 1TFA 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=1TFA OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10187803 10187803] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferrin]] | [[Category: 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 14:17:36 2008'' |
Revision as of 12:17, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
OVOTRANSFERRIN, N-TERMINAL LOBE, APO FORM
Overview
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 Structure
1TFA is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 14:17:36 2008
