1NAQ

Crystal structure of CUTA1 from E.coli at 1.7 A resolution

Summary for 1NAQ

• Entry DOI: 10.2210/pdb1naq/pdb
• Related: 1KR4
• Descriptor: Periplasmic divalent cation tolerance protein cutA, MERCURY (II) ION, MERCURIBENZOIC ACID, ... (4 entities in total)
• Functional Keywords: cuta, copper resistance, structural proteomics in europe, spine, structural genomics, electron transport
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P69488
• Total number of polymer chains: 6
• Total formula weight: 78873.90

Authors

Calderone, V.,Mangani, S.,Benvenuti, M.,Viezzoli, M.S.,Banci, L.,Bertini, I.,Structural Proteomics in Europe (SPINE) (deposition date: 2002-11-28, release date: 2003-11-25, Last modification date: 2024-02-14)

Primary citation

Arnesano, F.,Banci, L.,Benvenuti, M.,Bertini, I.,Calderone, V.,Mangani, S.,Viezzoli, M.S.
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.
J.Biol.Chem., 278:45999-46006, 2003

PubMed Abstract: 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 beta-sheet formation. Each subunit consists of a ferredoxin-like (beta1alpha1beta2beta3alpha2beta4) fold with an additional strand (beta5), a C-terminal helix (alpha3), and an unusual extended beta-hairpin involving strands beta2 and beta3. 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.

PubMed: 12949080
DOI: 10.1074/jbc.M304398200

Experimental method

X-RAY DIFFRACTION (1.7 Å)