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1naq

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(New page: 200px<br /><applet load="1naq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1naq, resolution 1.70&Aring;" /> '''Crystal structure of...)
Current revision (07:54, 14 February 2024) (edit) (undo)
 
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[[Image:1naq.gif|left|200px]]<br /><applet load="1naq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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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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==Overview==
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==Crystal structure of CUTA1 from E.coli at 1.7 A resolution==
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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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<StructureSection load='1naq' size='340' side='right'caption='[[1naq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1naq]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NAQ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MBO:MERCURIBENZOIC+ACID'>MBO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1naq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1naq OCA], [https://pdbe.org/1naq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1naq RCSB], [https://www.ebi.ac.uk/pdbsum/1naq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1naq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CUTA_ECOLI CUTA_ECOLI] Involved in resistance toward heavy metals.<ref>PMID:7623666</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/na/1naq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1naq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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 HG and MBO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NAQ OCA].
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*[[CutA1 3D structures|CutA1 3D structures]]
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== References ==
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==Reference==
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<references/>
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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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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Banci, L.]]
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[[Category: Banci L]]
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[[Category: Benvenuti, M.]]
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[[Category: Benvenuti M]]
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[[Category: Bertini, I.]]
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[[Category: Bertini I]]
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[[Category: Calderone, V.]]
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[[Category: Calderone V]]
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[[Category: Mangani, S.]]
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[[Category: Mangani S]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: Viezzoli MS]]
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[[Category: Viezzoli, M.S.]]
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[[Category: HG]]
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[[Category: MBO]]
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[[Category: copper resistance]]
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[[Category: cuta]]
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[[Category: spine]]
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[[Category: structural genomics]]
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[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:06:07 2007''
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Current revision

Crystal structure of CUTA1 from E.coli at 1.7 A resolution

PDB ID 1naq

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