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| | ==NMR structure of a downhill folding protein== | | ==NMR structure of a downhill folding protein== |
| - | <StructureSection load='2cyu' size='340' side='right' caption='[[2cyu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2cyu' size='340' side='right'caption='[[2cyu]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYU FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bbl|1bbl]], [[1bal|1bal]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [https://pdbe.org/2cyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [https://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://pdbe.org/2cyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). | + | [https://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). |
| | == 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== |
| - | *[[2-Oxoglutarate Dehydrogenase|2-Oxoglutarate Dehydrogenase]] | + | *[[2-oxoglutarate dehydrogenase 3D structures|2-oxoglutarate dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dihydrolipoyllysine-residue succinyltransferase]] | + | [[Category: Escherichia coli O157:H7]] |
| - | [[Category: Munoz, V]]
| + | [[Category: Large Structures]] |
| - | [[Category: Sadqi, M]] | + | [[Category: Munoz V]] |
| - | [[Category: Downhill folding protein]] | + | [[Category: Sadqi M]] |
| - | [[Category: Helix bundle]] | + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ODO2_ECO57 The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
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
Protein folding is an inherently complex process involving coordination of the intricate networks of weak interactions that stabilize native three-dimensional structures. In the conventional paradigm, simple protein structures are assumed to fold in an all-or-none process that is inaccessible to experiment. Existing experimental methods therefore probe folding mechanisms indirectly. A widely used approach interprets changes in protein stability and/or folding kinetics, induced by engineered mutations, in terms of the structure of the native protein. In addition to limitations in connecting energetics with structure, mutational methods have significant experimental uncertainties and are unable to map complex networks of interactions. In contrast, analytical theory predicts small barriers to folding and the possibility of downhill folding. These theoretical predictions have been confirmed experimentally in recent years, including the observation of global downhill folding. However, a key remaining question is whether downhill folding can indeed lead to the high-resolution analysis of protein folding processes. Here we show, with the use of nuclear magnetic resonance (NMR), that the downhill protein BBL from Escherichia coli unfolds atom by atom starting from a defined three-dimensional structure. Thermal unfolding data on 158 backbone and side-chain protons out of a total of 204 provide a detailed view of the structural events during folding. This view confirms the statistical nature of folding, and exposes the interplay between hydrogen bonding, hydrophobic forces, backbone conformation and side-chain entropy. From the data we also obtain a map of the interaction network in this protein, which reveals the source of folding cooperativity. Our approach can be extended to other proteins with marginal barriers (less than 3RT), providing a new tool for the study of protein folding.
Atom-by-atom analysis of global downhill protein folding.,Sadqi M, Fushman D, Munoz V Nature. 2006 Jul 20;442(7100):317-21. Epub 2006 Jun 14. PMID:16799571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sadqi M, Fushman D, Munoz V. Atom-by-atom analysis of global downhill protein folding. Nature. 2006 Jul 20;442(7100):317-21. Epub 2006 Jun 14. PMID:16799571 doi:10.1038/nature04859
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