2hc8

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Revision as of 18:18, 29 January 2008

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spinqualitylabelsall models 2hc8, resolution 1.650Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the A. fulgidus CopA A-domain

Overview

Copper homeostasis is maintained in part by membrane-bound P(1B)-type, ATPases that are found in all organisms and drive the transport of this, essential, yet toxic, metal ion across cellular membranes. CopA from, Archaeoglobus fulgidus is a hyperthermophilic member of this ATPase, subfamily and is homologous to the human Wilson and Menkes disease, ATPases. To gain insight into Cu(+)-ATPase function, the structure of the, CopA actuator domain (A-domain) was determined to 1.65 A resolution. The, CopA A-domain functions to couple ATP hydrolysis in the ATP binding domain, (ATPBD) with structural rearrangements of critical transmembrane segments., Its fold is quite similar to that of the sarcoplasmic reticulum, Ca(2+)-ATPase (SERCA1) A-domain, with the exception of an external loop, region. On the basis of sequence and structural comparisons, specific, residues that probably interact with the CopA ATPBD have been identified., Comparisons to the Wilson and Menkes disease A-domains reveal the presence, of an additional loop that may be associated with regulatory functions in, eukaryotic Cu(+)-ATPases. Finally, several mutations in the Wilson and, Menkes disease ATPases occur in the A-domain, and their likely effects on, function can be inferred from the CopA A-domain structure.

About this Structure

2HC8 is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase., Sazinsky MH, Agarwal S, Arguello JM, Rosenzweig AC, Biochemistry. 2006 Aug 22;45(33):9949-55. PMID:16906753

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