1naq

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[[Image:1naq.gif|left|200px]]<br /><applet load="1naq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1naq.gif|left|200px]]
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caption="1naq, resolution 1.70&Aring;" />
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'''Crystal structure of CUTA1 from E.coli at 1.7 A resolution'''<br />
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{{Structure
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|PDB= 1naq |SIZE=350|CAPTION= <scene name='initialview01'>1naq</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=MBO:MERCURIBENZOIC ACID'>MBO</scene>
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|ACTIVITY=
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|GENE= CUTA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of CUTA1 from E.coli at 1.7 A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NAQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=MBO:'>MBO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAQ OCA].
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1NAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAQ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12949080 12949080]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12949080 12949080]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: cuta]]
[[Category: cuta]]
[[Category: spine]]
[[Category: spine]]
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[[Category: structural genomics]]
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[[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 Thu Feb 21 14:04:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:20 2008''

Revision as of 10:54, 20 March 2008


PDB ID 1naq

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: and
Gene: CUTA (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of CUTA1 from E.coli at 1.7 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

1NAQ is a Single protein structure of sequence from Escherichia coli. 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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