2gt5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2gt5.gif|left|200px]] | [[Image:2gt5.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2gt5", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2gt5| PDB=2gt5 | SCENE= }} | |||
}} | |||
'''Solution structure of apo Human Sco1''' | '''Solution structure of apo Human Sco1''' | ||
| Line 34: | Line 31: | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
[[Category: | [[Category: Metalloprotein]] | ||
[[Category: | [[Category: Spine]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Structural proteomics in europe]] | ||
[[Category: | [[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 | |||
Revision as of 08:20, 13 April 2008
Solution structure of apo Human Sco1
OverviewOverview
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.
About this StructureAbout this Structure
2GT5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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 Page seeded by OCA on Sun Apr 13 08:20:04 2008