Yeast Ccc2 is a P-type ATPase responsible for transport of copper(I) from the cytosol to the trans-Golgi network. It possesses a soluble cytosolic N-terminal region containing two copper(I)-binding domains. Homologous eukaryotic copper-transporting ATPases have from one to six domains. We have expressed a fragment encompassing residues 1-150 of Ccc2, which corresponds to the two domains, and found that the second domain was substantially less structured than the first. The first domain could bind copper(I) and interact with the partner protein Atx1 at variance with the second. Similar results are found in ATPases from other organisms and may represent a general feature, whose biochemical implications are not yet fully appreciated. © 2007 Elsevier Inc. All rights reserved.

Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1 / L. Banci; I. Bertini; C.T. Chasapis; A. Rosato; L. Tenori. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 364:(2007), pp. 645-649. [10.1016/j.bbrc.2007.10.045]

Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1

BANCI, LUCIA;BERTINI, IVANO;ROSATO, ANTONIO;TENORI, LEONARDO
2007

Abstract

Yeast Ccc2 is a P-type ATPase responsible for transport of copper(I) from the cytosol to the trans-Golgi network. It possesses a soluble cytosolic N-terminal region containing two copper(I)-binding domains. Homologous eukaryotic copper-transporting ATPases have from one to six domains. We have expressed a fragment encompassing residues 1-150 of Ccc2, which corresponds to the two domains, and found that the second domain was substantially less structured than the first. The first domain could bind copper(I) and interact with the partner protein Atx1 at variance with the second. Similar results are found in ATPases from other organisms and may represent a general feature, whose biochemical implications are not yet fully appreciated. © 2007 Elsevier Inc. All rights reserved.
2007
364
645
649
L. Banci; I. Bertini; C.T. Chasapis; A. Rosato; L. Tenori
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/320231
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