| Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain. | |
| | |
MedLine Citation:
|
PMID: 19863064 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
The mechanism by which the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson disease (WD) protein for insertion into cuproenzymes is unclear. Using near-UV circular dichroism as a new tool to probe chaperone-target interactions, in combination with gel filtration and molecular dynamics simulations, we here demonstrate that Atox1 forms a stable Cu-dependent adduct with the fourth metal-binding domain of WD (WD4). Using point-mutated Atox1 variants, we show that the adduct forms in the absence of conserved residues M10 or T11 but K60 is essential for heterocomplex formation and Cu transfer. Dissection of heterocomplex energetic components reveals a crucial role for K60-mediated electrostatic interaction. |
| | |
Authors:
|
Faiza Hussain; Agustina Rodriguez-Granillo; Pernilla Wittung-Stafshede |
Related Documents
:
|
17482774 - The configuration of the cu(2+) binding region in full-length human prion protein compa... 12063264 - Yeast cox11, a protein essential for cytochrome c oxidase assembly, is a cu(i)-binding ... 14501004 - Characterization of radioiodinated ligand binding to amyloid beta plaques. 15911874 - Gm1 ganglioside and the seeding of amyloid in alzheimer's disease: endogenous seed for ... 22817714 - Copy number variations involving the microtubule-associated protein tau in human diseases. 15845444 - "sweet talk": closing in on c type lectin signaling. |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
|
Title: Journal of the American Chemical Society Volume: 131 ISSN: 1520-5126 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2009 Nov |
Date Detail:
|
Created Date: 2009-11-11 Completed Date: 2010-02-12 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
|
Languages: eng Pagination: 16371-3 Citation Subset: IM |
Affiliation:
|
Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, Texas 77251, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Adenosine Triphosphatases
/
chemistry* Cation Transport Proteins / chemistry* Computer Simulation Copper / chemistry* Humans Lysine / chemistry* Models, Chemical Models, Molecular Molecular Chaperones / chemistry* Protein Conformation |
| Chemical | |
Reg. No./Substance:
|
0/ATOX1 protein, human; 0/Cation Transport Proteins; 0/Molecular Chaperones; 56-87-1/Lysine; 7440-50-8/Copper; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.3.4/Wilson disease protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase.
Next Document: One-Dimensional Assembly of Silica Nanospheres Mediated by Block Copolymer in Liquid Phase.