1nft: Difference between revisions

Revision as of 15:26, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nft.png

Template:STRUCTURE 1nft

OVOTRANSFERRIN, N-TERMINAL LOBE, IRON LOADED OPEN FORMOVOTRANSFERRIN, N-TERMINAL LOBE, IRON LOADED OPEN FORM

Template:ABSTRACT PUBMED 10187803

About this StructureAbout this Structure

1NFT 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

Page seeded by OCA on Sun Jul 27 15:26:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1nft.gif|left|200px]]
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 {{STRUCTURE_1nft|  PDB=1nft  |  SCENE=  }}
-'''OVOTRANSFERRIN, N-TERMINAL LOBE, IRON LOADED OPEN FORM'''
+===OVOTRANSFERRIN, N-TERMINAL LOBE, IRON LOADED OPEN 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10187803}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10187803 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10187803}}
 ==About this Structure==
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 [[Category: Ovotransferrin]]
 [[Category: Transferrin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:28:50 2008''
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