|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of rat CUTA1 at 2.15 A resolution== | | ==Crystal structure of rat CUTA1 at 2.15 A resolution== |
| - | <StructureSection load='1osc' size='340' side='right' caption='[[1osc]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='1osc' size='340' side='right'caption='[[1osc]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1osc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OSC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1osc]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OSC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kr4|1kr4]], [[1naq|1naq]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CutA, CutA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1osc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osc OCA], [https://pdbe.org/1osc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1osc RCSB], [https://www.ebi.ac.uk/pdbsum/1osc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1osc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1osc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osc OCA], [http://pdbe.org/1osc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1osc RCSB], [http://www.ebi.ac.uk/pdbsum/1osc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1osc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CUTA_RAT CUTA_RAT]] May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE). | + | [https://www.uniprot.org/uniprot/CUTA_RAT CUTA_RAT] May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 28: |
| | </div> | | </div> |
| | <div class="pdbe-citations 1osc" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1osc" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[CutA1 3D structures|CutA1 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Arnesano, F]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Banci, L]] | + | [[Category: Arnesano F]] |
| - | [[Category: Benvenuti, M]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I]] | + | [[Category: Benvenuti M]] |
| - | [[Category: Calderone, V]] | + | [[Category: Bertini I]] |
| - | [[Category: Mangani, S]] | + | [[Category: Calderone V]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Mangani S]] |
| - | [[Category: Viezzoli, M S]] | + | [[Category: Viezzoli MS]] |
| - | [[Category: Copper resistance]]
| + | |
| - | [[Category: Cuta]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arnesano F, Banci L, Benvenuti M, Bertini I, Calderone V, Mangani S, Viezzoli MS. The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction. J Biol Chem. 2003 Nov 14;278(46):45999-6006. Epub 2003 Aug 29. PMID:12949080 doi:http://dx.doi.org/10.1074/jbc.M304398200
|
