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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Banci L,Bertini I,Chasapis CT,Rosato A,Tenori L

doi

10.1016/j.bbrc.2007.10.045

subject

Has Abstract

pub_date

2007-12-21 00:00:00

pages

645-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)02219-X

journal_volume

364

pub_type

杂志文章

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