1osc

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{{STRUCTURE_1osc| PDB=1osc | SCENE= }}
{{STRUCTURE_1osc| PDB=1osc | SCENE= }}
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'''Crystal structure of rat CUTA1 at 2.15 A resolution'''
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===Crystal structure of rat CUTA1 at 2.15 A resolution===
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==Overview==
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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 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.
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{{ABSTRACT_PUBMED_12949080}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:09:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:34:08 2008''

Revision as of 02:34, 29 July 2008

Image:1osc.png

Template:STRUCTURE 1osc

Crystal structure of rat CUTA1 at 2.15 A resolution

Template:ABSTRACT PUBMED 12949080

About this Structure

1OSC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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

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