1iq7: Difference between revisions

Revision as of 13:47, 1 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:1iq7.png

Template:STRUCTURE 1iq7

Ovotransferrin, C-Terminal Lobe, Apo FormOvotransferrin, C-Terminal Lobe, Apo Form

Template:ABSTRACT PUBMED 11466309

About this StructureAbout this Structure

1IQ7 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Anion-mediated Fe3+ release mechanism in ovotransferrin C-lobe: a structurally identified SO4(2-) binding site and its implications for the kinetic pathway., Mizutani K, Muralidhara BK, Yamashita H, Tabata S, Mikami B, Hirose M, J Biol Chem. 2001 Sep 21;276(38):35940-6. Epub 2001 Jul 20. PMID:11466309

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OCA

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 {{STRUCTURE_1iq7|  PDB=1iq7  |  SCENE=  }}
-'''Ovotransferrin, C-Terminal Lobe, Apo Form'''
+===Ovotransferrin, C-Terminal Lobe, Apo Form===
-==Overview==
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-The differential properties of anion-mediated Fe(3+) release between the N- and C-lobes of transferrins have been a focus in transferrin biochemistry. The structural and kinetic characteristics for isolated lobe have, however, been documented with the N-lobe only. Here we demonstrate for the first time the quantitative Fe(3+) release kinetics and the anion-binding structure for the isolated C-lobe of ovotransferrin. In the presence of pyrophosphate, sulfate, and nitrilotriacetate anions, the C-lobe released Fe(3+) with a decelerated rate in a single exponential progress curve, and the observed first order rate constants displayed a hyperbolic profile as a function of the anion concentration. The profile was consistent with a newly derived single-pathway Fe(3+) release model in which the holo form is converted depending on the anion concentration into a "mixed ligand" intermediate that releases Fe(3+). The apo C-lobe was crystallized in ammonium sulfate solution, and the structure determined at 2.3 A resolution demonstrated the existence of a single bound SO(4)(2-) in the interdomain cleft, which interacts directly with Thr(461)-OG1, Tyr(431)-OH, and His(592)-NE2 and indirectly with Tyr(524)-OH. The latter three groups are Fe(3+)-coordinating ligands, strongly suggesting the facilitated Fe(3+) release upon the anion occupation at this site. The SO(4)(2-) binding structure supported the single-pathway kinetic model.
+The line below this paragraph, {{ABSTRACT_PUBMED_11466309}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11466309 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11466309}}
 ==About this Structure==
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 [[Category: Transferrin]]
 [[Category: Transport protein]]
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