2ggt: Difference between revisions

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[[Image:2ggt.gif|left|200px]]
{{Seed}}
[[Image:2ggt.png|left|200px]]


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{{STRUCTURE_2ggt|  PDB=2ggt  |  SCENE=  }}  
{{STRUCTURE_2ggt|  PDB=2ggt  |  SCENE=  }}  


'''Crystal structure of human SCO1 complexed with nickel.'''
===Crystal structure of human SCO1 complexed with nickel.===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16735468}}


==Disease==
==Disease==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16735468 16735468]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16735468 16735468]
Crystal structure of human SCO1: implications for redox signaling by a mitochondrial cytochrome c oxidase "assembly" protein., Williams JC, Sue C, Banting GS, Yang H, Glerum DM, Hendrickson WA, Schon EA, J Biol Chem. 2005 Apr 15;280(15):15202-11. Epub 2005 Jan 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15659396 15659396]
Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assembly., Balatri E, Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Structure. 2003 Nov;11(11):1431-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14604533 14604533]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Nickel]]
[[Category: Nickel]]
[[Category: Redox]]
[[Category: Redox]]
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