1OSC

Crystal structure of rat CUTA1 at 2.15 A resolution

1OSC の概要

• エントリーDOI: 10.2210/pdb1osc/pdb
• 関連するPDBエントリー: 1KR4 1NAQ
• 分子名称: similar to divalent cation tolerant protein CUTA (2 entities in total)
• 機能のキーワード: cuta, copper resistance, structural proteomics in europe, spine, structural genomics, unknown function
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 81603.11

構造登録者

Arnesano, F.,Banci, L.,Benvenuti, M.,Bertini, I.,Calderone, V.,Mangani, S.,Viezzoli, M.S.,Structural Proteomics in Europe (SPINE) (登録日: 2003-03-19, 公開日: 2003-11-25, 最終更新日: 2023-08-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)