1zy8

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{{Large structure}}
 
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{{STRUCTURE_1zy8| PDB=1zy8 | SCENE= }}
 
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===The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.===
 
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{{ABSTRACT_PUBMED_16263718}}
 
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==Disease==
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==The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.==
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[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Note=Defects in DLD are involved in the development of congenital infantile lactic acidosis. Defects in DLD are a cause of maple syrup urine disease (MSUD) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation. [[http://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN]] Defects in PDHX are the cause of pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:[http://omim.org/entry/245349 245349]].<ref>PMID:9399911</ref>
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<StructureSection load='1zy8' size='340' side='right'caption='[[1zy8]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zy8]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZY8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59&#8491;, 2 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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=1zy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy8 OCA], [https://pdbe.org/1zy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1zy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zy8 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN] Note=Defects in DLD are involved in the development of congenital infantile lactic acidosis. Defects in DLD are a cause of maple syrup urine disease (MSUD) [MIM:[https://omim.org/entry/248600 248600]. MSUD is characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation.
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== Function ==
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[https://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/1zy8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1zy8 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The dihydrolipoamide dehydrogenase-binding protein (E3BP) and the dihydrolipoamide acetyltransferase (E2) component enzyme form the structural core of the human pyruvate dehydrogenase complex by providing the binding sites for two other component proteins, dihydrolipoamide dehydrogenase (E3) and pyruvate dehydrogenase (E1), as well as pyruvate dehydrogenase kinases and phosphatases. Despite a high similarity between the primary structures of E3BP and E2, the E3-binding domain of human E3BP is highly specific to human E3, whereas the E1-binding domain of human E2 is highly specific to human E1. In this study, we characterized binding of human E3 to the E3-binding domain of E3BP by x-ray crystallography at 2.6-angstroms resolution, and we used this structural information to interpret the specificity for selective binding. Two subunits of E3 form a single recognition site for the E3-binding domain of E3BP through their hydrophobic interface. The hydrophobic residues Pro133, Pro154, and Ile157 in the E3-binding domain of E3BP insert themselves into the surface of both E3 polypeptide chains. Numerous ionic and hydrogen bonds between the residues of three interacting polypeptide chains adjacent to the central hydrophobic patch add to the stability of the subcomplex. The specificity of pairing for human E3BP with E3 is interpreted from its subcomplex structure to be most likely due to conformational rigidity of the binding fragment of the E3-binding domain of E3BP and its exquisite amino acid match with the E3 target interface.
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==Function==
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How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.,Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. PMID:16263718<ref>PMID:16263718</ref>
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[[http://www.uniprot.org/uniprot/DLDH_HUMAN DLDH_HUMAN]] Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction. [[http://www.uniprot.org/uniprot/ODPX_HUMAN ODPX_HUMAN]] Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[1zy8]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZY8 OCA].
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</div>
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<div class="pdbe-citations 1zy8" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
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*[[Pyruvate dehydrogenase|Pyruvate dehydrogenase]]
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*[[Pyruvate dehydrogenase 3D structures|Pyruvate dehydrogenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016263718</ref><references group="xtra"/><references/>
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__TOC__
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[[Category: Dihydrolipoyl dehydrogenase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ciszak, E M.]]
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[[Category: Large Structures]]
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[[Category: Hong, Y S.]]
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[[Category: Ciszak EM]]
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[[Category: Korotchkina, L G.]]
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[[Category: Hong YS]]
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[[Category: Makal, A.]]
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[[Category: Korotchkina LG]]
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[[Category: Patel, M S.]]
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[[Category: Makal A]]
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[[Category: Vettaikkorumakankauv, A K.]]
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[[Category: Patel MS]]
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[[Category: Alpha-keto acid complex]]
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[[Category: Vettaikkorumakankauv AK]]
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[[Category: Dihydrolipoamide dehydrogenase]]
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[[Category: Dihydrolipoamide dehydrogenase binding protein]]
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[[Category: Dihydrolipoyl dehydrogenase]]
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[[Category: E3]]
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[[Category: E3-binding protein]]
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[[Category: Flavin adenine dinucleotide cofactor]]
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[[Category: Human]]
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[[Category: Oxidoreductase]]
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[[Category: Pyruvate dehydrogenase complex]]
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Current revision

The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.

PDB ID 1zy8

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