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| | <StructureSection load='1b5s' size='340' side='right'caption='[[1b5s]], [[Resolution|resolution]] 4.40Å' scene=''> | | <StructureSection load='1b5s' size='340' side='right'caption='[[1b5s]], [[Resolution|resolution]] 4.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b5s]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The September 2012 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pyruvate Dehydrogenase Complex'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2012_9 10.2210/rcsb_pdb/mom_2012_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B5S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b5s]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. The September 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Pyruvate Dehydrogenase Complex'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_9 10.2210/rcsb_pdb/mom_2012_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5S FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></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]] 4.4Å</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=1b5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5s OCA], [http://pdbe.org/1b5s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b5s RCSB], [http://www.ebi.ac.uk/pdbsum/1b5s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5s 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=1b5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5s OCA], [https://pdbe.org/1b5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5s RCSB], [https://www.ebi.ac.uk/pdbsum/1b5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5s ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). | + | [https://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | |
| | [[Category: Geobacillus stearothermophilus]] | | [[Category: Geobacillus stearothermophilus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Pyruvate Dehydrogenase Complex]] | | [[Category: Pyruvate Dehydrogenase Complex]] |
| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| - | [[Category: Aevarsson, A]] | + | [[Category: Aevarsson A]] |
| - | [[Category: Allen, M D]] | + | [[Category: Allen MD]] |
| - | [[Category: Hol, W G]] | + | [[Category: De Kok A]] |
| - | [[Category: Izard, T]] | + | [[Category: Hol WG]] |
| - | [[Category: Kok, A De]] | + | [[Category: Izard T]] |
| - | [[Category: Perham, R N]] | + | [[Category: Perham RN]] |
| - | [[Category: Westphal, A H]] | + | [[Category: Westphal AH]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Dihydrolipoyl acetyltransferase]]
| + | |
| - | [[Category: Dihydrolipoyl transacetylase]]
| + | |
| - | [[Category: E2p]]
| + | |
| - | [[Category: Pyruvate dehydrogenase]]
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| Structural highlights
Function
ODP2_GEOSE The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
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
The pyruvate dehydrogenase multienzyme complex (Mr of 5-10 million) is assembled around a structural core formed of multiple copies of dihydrolipoyl acetyltransferase (E2p), which exhibits the shape of either a cube or a dodecahedron, depending on the source. The crystal structures of the 60-meric dihydrolipoyl acyltransferase cores of Bacillus stearothermophilus and Enterococcus faecalis pyruvate dehydrogenase complexes were determined and revealed a remarkably hollow dodecahedron with an outer diameter of approximately 237 A, 12 large openings of approximately 52 A diameter across the fivefold axes, and an inner cavity with a diameter of approximately 118 A. Comparison of cubic and dodecahedral E2p assemblies shows that combining the principles of quasi-equivalence formulated by Caspar and Klug [Caspar, D. L. & Klug, A. (1962) Cold Spring Harbor Symp. Quant. Biol. 27, 1-4] with strict Euclidean geometric considerations results in predictions of the major features of the E2p dodecahedron matching the observed features almost exactly.
Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes.,Izard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1240-5. PMID:9990008[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Izard T, Aevarsson A, Allen MD, Westphal AH, Perham RN, de Kok A, Hol WG. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1240-5. PMID:9990008
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