1p6t

File:1p6t.gif

spinqualitylabelsall models 1p6t Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis

OverviewOverview

The solution structure of the N-terminal region (151 amino acids) of a, copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists, of two domains, CopAa and CopAb, linked by two amino acids. It is found, that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few, hydrophobic interactions, forming a single rigid body. The two metal, binding sites are far from one another, and the short link between the, domains prevents them from interacting. This and the surface electrostatic, potential suggest that each domain receives copper from the copper, chaperone, CopZ, independently and transfers it to the membrane binding, site of CopA. The affinity constants of silver(I) and copper(I) are, similar for the two sites as monitored by NMR. Because the present, construct "domain-short link-domain" is shared also by the last two, domains of the eukaryotic copper ATPases and several residues at the, interface between the two domains are conserved, the conclusions of the, present study have general validity for the understanding of the function, of copper ATPases.

About this StructureAbout this Structure

1P6T is a Single protein structure of sequence from Bacillus subtilis. Active as Copper-exporting ATPase, with EC number 3.6.3.4 Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis., Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC, J Biol Chem. 2003 Dec 12;278(50):50506-13. Epub 2003 Sep 27. PMID:14514665

Page seeded by OCA on Tue Nov 20 23:31:45 2007