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Abstract:

The molecular details of how copper (Cu) is transferred from the human Cu chaperone Atox1 to metalbinding domains (MBDs) of P1B-type ATPases are still unclear. Here, we use a computational approach, employing quantum mechanics/molecular mechanics (QM/MM) methods, to shed light on the reaction mechanism [probable intermediates, Cu(I) coordination geometries, activation barriers, and energetics] of Cu(I) transfer from Atox1 to the fourth MBD of Wilson disease protein (WD4). Both Atox1 and WD4 have solvent-exposed metal-binding motifs with two Cys residues that coordinate Cu(I). After assessing the existence of all possible 2-, 3- and 4-coordinate Cu-intermediate species, one dominant reaction path emerged. First, without activation barrier, WD4's Cys1 binds Cu(I) in Atox1 to form a 3-coordinated intermediate. Next, with an activation barrier of about 9.5 kcal/mol, a second 3-coordinated intermediate forms that involves both of the Cys residues in WD4 and Cys1 of Atox1. This species can then form the product by decoordination of Atox1's Cys1 (barrier of about 8 kcal/mol). Overall, the Cu-transfer reaction from Atox1 to WD4 appears to be kinetically accessible but less energetically favorable (△E = 7.7 kcal/mol). Our results provide unique insights into the molecular mechanism of protein-mediated Cu(I) transfer in the secretory pathway and are in agreement with existing experimental data. © 2010 American Chemical Society.

Registro:

Documento: Artículo
Título:Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein
Autor:Rodriguez-Granillo, A.; Crespo, A.; Estrin, D.A.; Wittung-Stafshede, P.
Filiación:Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251, United States
Department of Bioengineering, Rice University, Houston, TX 77005, United States
Chemistry Modeling and Informatics, Merck Research Laboratories, Rahway, NJ 07065, United States
Departamento de Química Inorgánica, Analítica y Química-Física, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pab. 2, C1428EHA Buenos Aires, Argentina
Department of Chemistry, Umeå University, 90187 Umeå, Sweden
Palabras clave:Coordination reactions; Activation barriers; ATPases; Computational approach; Coordination geometry; Cys residues; Experimental data; Intermediate specie; Metal binding domain; Metal-binding motif; Molecular mechanism; Reaction mechanism; Reaction paths; Secretory pathways; Transfer mechanisms; Transfer reaction; Wilson disease; Reaction intermediates; adenosine triphosphatase; ATOX1 protein, human; cation transport protein; chaperone; copper; metal; Wilson disease protein; article; chemistry; human; metabolism; molecular dynamics; protein binding; protein tertiary structure; quantum theory; thermodynamics; Adenosine Triphosphatases; Cation Transport Proteins; Copper; Humans; Metals; Molecular Chaperones; Molecular Dynamics Simulation; Protein Binding; Protein Structure, Tertiary; Quantum Theory; Thermodynamics
Año:2010
Volumen:114
Número:10
Página de inicio:3698
Página de fin:3706
DOI: http://dx.doi.org/10.1021/jp911208z
Título revista:Journal of Physical Chemistry B
Título revista abreviado:J Phys Chem B
ISSN:15206106
CODEN:JPCBF
CAS:adenosine triphosphatase, 37289-25-1, 9000-83-3; copper, 15158-11-9, 7440-50-8; ATOX1 protein, human; Adenosine Triphosphatases, 3.6.1.-; Cation Transport Proteins; Copper, 7440-50-8; Metals; Molecular Chaperones; Wilson disease protein, 3.6.3.4
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n10_p3698_RodriguezGranillo

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Citas:

---------- APA ----------
Rodriguez-Granillo, A., Crespo, A., Estrin, D.A. & Wittung-Stafshede, P. (2010) . Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein. Journal of Physical Chemistry B, 114(10), 3698-3706.
http://dx.doi.org/10.1021/jp911208z
---------- CHICAGO ----------
Rodriguez-Granillo, A., Crespo, A., Estrin, D.A., Wittung-Stafshede, P. "Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein" . Journal of Physical Chemistry B 114, no. 10 (2010) : 3698-3706.
http://dx.doi.org/10.1021/jp911208z
---------- MLA ----------
Rodriguez-Granillo, A., Crespo, A., Estrin, D.A., Wittung-Stafshede, P. "Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein" . Journal of Physical Chemistry B, vol. 114, no. 10, 2010, pp. 3698-3706.
http://dx.doi.org/10.1021/jp911208z
---------- VANCOUVER ----------
Rodriguez-Granillo, A., Crespo, A., Estrin, D.A., Wittung-Stafshede, P. Copper-transfer mechanism from the human chaperone Atox1 to a metal-binding domain of wilson disease protein. J Phys Chem B. 2010;114(10):3698-3706.
http://dx.doi.org/10.1021/jp911208z