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3rqc

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Crystal structure of the catalytic core of the 2-oxoacid dehydrogenase multienzyme complex from Thermoplasma acidophilum

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Retrieved from "http://52.214.119.220/wiki/index.php/3rqc"

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 <StructureSection load='3rqc' size='340' side='right'caption='[[3rqc]], [[Resolution|resolution]] 4.01&Aring;' scene=''>
 == 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]] 4.01&#8491;</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>
 <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>
-<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>
-From MEDLINE&reg;/PubMed&reg;, 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__
 </StructureSection>
 [[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]]

3rqc

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Crystal structure of the catalytic core of the 2-oxoacid dehydrogenase multienzyme complex from Thermoplasma acidophilum

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