2gql: Difference between revisions
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|PDB= 2gql |SIZE=350|CAPTION= <scene name='initialview01'>2gql</scene> | |PDB= 2gql |SIZE=350|CAPTION= <scene name='initialview01'>2gql</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SCO1, SCOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SCO1, SCOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2gqk|2GQK]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gql OCA], [http://www.ebi.ac.uk/pdbsum/2gql PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gql RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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 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 Structure== | ==About this Structure== | ||
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[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
[[Category: spine]] | [[Category: spine]] | ||
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[[Category: thioredoxin-like fold]] | [[Category: thioredoxin-like fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:20:11 2008'' | ||