2gt5: Difference between revisions

Revision as of 13:11, 29 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:2gt5.png

Template:STRUCTURE 2gt5

Solution structure of apo Human Sco1Solution structure of apo Human Sco1

Template:ABSTRACT PUBMED 16735468

About this StructureAbout this Structure

2GT5 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

A hint for the function of human Sco1 from different structures., Banci L, Bertini I, Calderone V, Ciofi-Baffoni S, Mangani S, Martinelli M, Palumaa P, Wang S, Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8595-600. Epub 2006 May 30. PMID:16735468

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

OCA

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-[[Image:2gt5.gif|left|200px]]
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 {{STRUCTURE_2gt5|  PDB=2gt5  |  SCENE=  }}
-'''Solution structure of apo Human Sco1'''
+===Solution structure of apo Human Sco1===
-==Overview==
+<!--
-The solution structures of apo, Cu(I), and Ni(II) human Sco1 have been determined. The protein passes from an open and conformationally mobile state to a closed and rigid conformation upon metal binding as shown by electrospray ionization MS and NMR data. The metal ligands of Cu(I) are two Cys residues of the CPXXCP motif and a His residue. The latter is suitably located to coordinate the metal anchored by the two Cys residues. The coordination sphere of Ni(II) in solution is completed by another ligand, possibly Asp. Crystals of the Ni(II) derivative were also obtained with the Ni(II) ion bound to the same His residue and to the two oxidized Cys residues of the CPXXCP motif. We propose that the various structures solved here represent the various states of the protein in its functional cycle and that the metal can be bound to the oxidized protein at a certain stage. Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function.
+The line below this paragraph, {{ABSTRACT_PUBMED_16735468}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16735468 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16735468}}
 ==About this Structure==
-GT5 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=2GT5 OCA].
+GT5 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=2GT5 OCA].
 ==Reference==
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 [[Category: Structural proteomics in europe]]
 [[Category: Thioredoxin-like fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:20:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:11:20 2008''