2gql
From Proteopedia
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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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Hepatic failure, early onset, and neurologic disorder OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603644 603644]] | ||
==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: NI]] | ||
[[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'' |
Revision as of 00:20, 31 March 2008
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| Ligands: | |||||||
| Gene: | SCO1, SCOD1 (Homo sapiens) | ||||||
| Related: | 2GQK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of Human Ni(II)-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.
About this Structure
2GQL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
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:16735468
Page seeded by OCA on Mon Mar 31 03:20:11 2008
Categories: Homo sapiens | Single protein | Banci, L. | Bertini, I. | Calderone, V. | Ciofi-Baffoni, S. | Mangani, S. | Martinelli, M. | Palumaa, P. | SPINE, Structural Proteomics in Europe. | Wang, S. | Metalloprotein | Spine | Structural genomic | Structural proteomics in europe | Thioredoxin-like fold
