1osc

Crystal structure of rat CUTA1 at 2.15 A resolution

spinqualitylabelsall models 1osc, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1osc is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CUTA_RAT May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction.,Arnesano F, Banci L, Benvenuti M, Bertini I, Calderone V, Mangani S, Viezzoli MS J Biol Chem. 2003 Nov 14;278(46):45999-6006. Epub 2003 Aug 29. PMID:12949080 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CutA1 3D structures

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