2hrf: Difference between revisions

Revision as of 19:03, 28 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:2hrf.png

Template:STRUCTURE 2hrf

Solution Structure of Cu(I) P174L HSco1Solution Structure of Cu(I) P174L HSco1

Template:ABSTRACT PUBMED 17182746

About this StructureAbout this Structure

2HRF is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Human Sco1 functional studies and pathological implications of the P174L mutant., Banci L, Bertini I, Ciofi-Baffoni S, Leontari I, Martinelli M, Palumaa P, Sillard R, Wang S, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):15-20. Epub 2006 Dec 20. PMID:17182746

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 {{STRUCTURE_2hrf|  PDB=2hrf  |  SCENE=  }}
-'''Solution Structure of Cu(I) P174L HSco1'''
+===Solution Structure of Cu(I) P174L HSco1===
-==Overview==
+<!--
-The pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding site and causes a reduction of the affinity of copper(I) for the protein. K(D) values for Cu(I)WT-HSco1 and Cu(I)P174L-HSco1 are approximately 10(-17) and approximately 10(-13), respectively. The reduction potentials of the two apo proteins are similar, but slower reduction/oxidation rates are found for the mutant with respect to the WT. The mitochondrial metallochaperone in the partially oxidized Cu(1)(I)Cox17(2S-S) form, at variance with the fully reduced Cu(4)(I)Cox17, interacts transiently with both WT-HSco1 and the mutant, forming the Cox17/Cu(I)/HSco1 complex, but copper is efficiently transferred only in the case of WT protein. Cu(1)(I)Cox17(2S-S) indeed has an affinity for copper(I) (K(D) approximately 10(-15)) higher than that of the P174L-HSco1 mutant but lower than that of WT-HSco1. We propose that HSco1 mutation, altering the structure around the metal-binding site, affects both copper(I) binding and redox properties of the protein, thus impairing the efficiency of copper transfer to CcO. The pathogenic mutation therefore could (i) lessen the Sco1 affinity for copper(I) and hence copper supply for CcO or (ii) decrease the efficiency of reduction of CcO thiols involved in copper binding, or both effects could be produced by the mutation.
+The line below this paragraph, {{ABSTRACT_PUBMED_17182746}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17182746 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17182746}}
 ==About this Structure==
-HRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRF OCA].
+HRF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRF OCA].
 ==Reference==
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 [[Category: Structural genomic]]
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