1iyu
From Proteopedia
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==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE== | ==LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE== | ||
| - | <StructureSection load='1iyu' size='340' side='right'caption='[[1iyu | + | <StructureSection load='1iyu' size='340' side='right'caption='[[1iyu]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYU FirstGlance]. <br> | <table><tr><td colspan='2'>[[1iyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYU FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1iyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyu OCA], [https://pdbe.org/1iyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyu RCSB], [https://www.ebi.ac.uk/pdbsum/1iyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyu 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=1iyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyu OCA], [https://pdbe.org/1iyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyu RCSB], [https://www.ebi.ac.uk/pdbsum/1iyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ODP2_AZOVI ODP2_AZOVI] 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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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iyu ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iyu ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The three-dimensional structure of the N-terminal lipoyl domain of the acetyltransferase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii has been determined using heteronuclear multidimensional NMR spectroscopy and dynamical simulated annealing. The structure is compared with the solution structure of the lipoyl domain of the A. vinelandii 2-oxoglutarate dehydrogenase complex. The overall fold of the two structures, described as a beta-barrel-sandwich hybrid, is very similar. This agrees well with the high similarity of NMR-derived parameters, e.g. chemical shifts, between the two lipoyl domains. The main structural differences between the two lipoyl domains occur in a solvent-exposed loop close in space to the lipoylation site. Despite their high structural similarity, these lipoyl domains show a high preference for being reductively acylated by their parent 2-oxo acid dehydrogenase. Potential residues of the lipoyl domain involved in this process of molecular recognition are discussed. | ||
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| - | Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.,Berg A, Vervoort J, de Kok A Eur J Biochem. 1997 Mar 1;244(2):352-60. PMID:9119000<ref>PMID:9119000</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1iyu" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Dihydrolipoamide acetyltransferase|Dihydrolipoamide acetyltransferase]] | + | *[[Dihydrolipoamide acetyltransferase 3D structures|Dihydrolipoamide acetyltransferase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
| - | [[Category: Dihydrolipoyllysine-residue acetyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berg | + | [[Category: Berg A]] |
| - | [[Category: Kok | + | [[Category: De Kok A]] |
| - | [[Category: Vervoort | + | [[Category: Vervoort J]] |
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Revision as of 07:49, 3 April 2024
LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
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