1osc
From Proteopedia
(New page: 200px<br /><applet load="1osc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osc, resolution 2.15Å" /> '''Crystal structure of...) |
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| - | [[Image:1osc.jpg|left|200px]]<br /><applet load="1osc" size=" | + | [[Image:1osc.jpg|left|200px]]<br /><applet load="1osc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1osc, resolution 2.15Å" /> | caption="1osc, resolution 2.15Å" /> | ||
'''Crystal structure of rat CUTA1 at 2.15 A resolution'''<br /> | '''Crystal structure of rat CUTA1 at 2.15 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 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 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1OSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Calderone, V.]] | [[Category: Calderone, V.]] | ||
[[Category: Mangani, S.]] | [[Category: Mangani, S.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
| - | [[Category: Viezzoli, M | + | [[Category: Viezzoli, M S.]] |
[[Category: copper resistance]] | [[Category: copper resistance]] | ||
[[Category: cuta]] | [[Category: cuta]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:01 2008'' |
Revision as of 12:21, 21 February 2008
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Crystal structure of rat CUTA1 at 2.15 A resolution
Overview
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.
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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