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| | <StructureSection load='3rqc' size='340' side='right'caption='[[3rqc]], [[Resolution|resolution]] 4.01Å' scene=''> | | <StructureSection load='3rqc' size='340' side='right'caption='[[3rqc]], [[Resolution|resolution]] 4.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rqc]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Theac Theac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rqc]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum_DSM_1728 Thermoplasma acidophilum DSM 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQC FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ta1436 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 THEAC])</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]] 4.01Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></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=3rqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqc OCA], [https://pdbe.org/3rqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rqc RCSB], [https://www.ebi.ac.uk/pdbsum/3rqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rqc ProSAT]</span></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=3rqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqc OCA], [https://pdbe.org/3rqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rqc RCSB], [https://www.ebi.ac.uk/pdbsum/3rqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rqc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q9HIA5_THEAC Q9HIA5_THEAC] |
| - | The dihydrolipoyl acyl-transferase (E2) enzyme forms the structural and catalytic core of the tripartite 2-oxoacid dehydrogenase multienzyme complexes of the central metabolic pathways. Although this family of multienzyme complexes shares a common architecture, their E2 cores form homo-trimers that, depending on the source, further associate into either octahedral (24-mer) or icosahedral (60-mer) assemblies, as predicted by the principles of quasi-equivalence. In the crystal structure of the E2 core from Thermoplasma acidophilum, a thermophilic archaeon, the homo-trimers assemble into a unique 42-mer oblate spheroid. Analytical equilibrium centrifugation and small-angle X-ray scattering analyses confirm that this catalytically active 1.08 MDa assembly exists as a single species in solution, forming a hollow spheroid with a maximum diameter of 220 A. In this paper we show that a monodisperse macromolecular assembly, built from identical subunits in non-identical environments, forms an irregular protein shell via non-equivalent interactions. This unusually irregular protein shell, combining cubic and dodecahedral geometrical elements, expands on the concept of quasi-equivalence as a basis for understanding macromolecular assemblies by showing that cubic point group symmetry is not a physical requirement in multienzyme assembly. These results extend our basic knowledge of protein assembly and greatly expand the number of possibilities to manipulate self-assembling biological complexes to be utilized in innovative nanotechnology applications.
| + | |
| - | | + | |
| - | The catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assembly.,Marrott NL, Marshall JJ, Svergun DI, Crennell SJ, Hough DW, Danson MJ, van den Elsen JM FEBS J. 2012 Mar;279(5):713-23. doi: 10.1111/j.1742-4658.2011.08461.x. Epub 2012 , Jan 19. PMID:22188654<ref>PMID:22188654</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3rqc" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Theac]] | + | [[Category: Thermoplasma acidophilum DSM 1728]] |
| - | [[Category: Crennell, S J]] | + | [[Category: Crennell SJ]] |
| - | [[Category: Danson, M J]] | + | [[Category: Danson MJ]] |
| - | [[Category: Elsen, J M.H van den]]
| + | [[Category: Hough DW]] |
| - | [[Category: Hough, D W]] | + | [[Category: Marrott NL]] |
| - | [[Category: Marrott, N L]] | + | [[Category: Van den Elsen JMH]] |
| - | [[Category: Acyl-transferase]] | + | |
| - | [[Category: Alpha beta fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
