Journal of Biological Chemistry
Volume 278, Issue 46, 14 November 2003, Pages 45999-46006
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Protein Structure and Folding
The Evolutionarily Conserved Trimeric Structure of CutA1 Proteins Suggests a Role in Signal Transduction*

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CutA1 are a protein family present in bacteria, plants, and animals, including humans. Escherichia coli CutA1 is involved in copper tolerance, whereas mammalian proteins are implicated in the anchoring of acetylcholinesterase in neuronal cell membranes. The x-ray structures of CutA1 from E. coli and rat were determined. Both proteins are trimeric in the crystals and in solution through an inter-subunit β-sheet formation. Each subunit consists of a ferredoxin-like (β1α1β2β3α2β4) fold with an additional strand (β5), a C-terminal helix (α3), and an unusual extended β-hairpin involving strands β2 and β3. The bacterial CutA1 is able to bind copper(II) in vitro through His2Cys coordination in a type II water-accessible site, whereas the rat protein precipitates in the presence of copper(II). The evolutionarily conserved trimeric assembly of CutA1 is reminiscent of the architecture of PII signal transduction proteins. This similarity suggests an intriguing role of CutA1 proteins in signal transduction through allosteric communications between subunits.

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The atomic coordinates and structure factors (code 1NAQ (E. coli) and 1OSC (rat CutA1)) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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This work has been supported by European Commission Contracts HPRI-CT-2001-50028 and QLG2-CT-2002-00988, European Community Access to European Molecular Biology Laboratory Hamburg Outstation Contract HPRI-CT-1999-00017, and Italian Ministero dell'Università e della Ricerca Scientifica e Tecnologica Project COFIN01. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1 and 2.