1zy8

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[[Image:1zy8.gif|left|200px]]
[[Image:1zy8.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1zy8 |SIZE=350|CAPTION= <scene name='initialview01'>1zy8</scene>, resolution 2.59&Aring;
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The line below this paragraph, containing "STRUCTURE_1zy8", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= DLD, GCSL, LAD, PHE3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), PDHX, PDX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1zy8| PDB=1zy8 | SCENE= }}
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|RELATEDENTRY=[[1ni4|1ni4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zy8 OCA], [http://www.ebi.ac.uk/pdbsum/1zy8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zy8 RCSB]</span>
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}}
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'''The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.'''
'''The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.'''
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[[Category: Patel, M S.]]
[[Category: Patel, M S.]]
[[Category: Vettaikkorumakankauv, A K.]]
[[Category: Vettaikkorumakankauv, A K.]]
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[[Category: alpha-keto acid complex]]
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[[Category: Alpha-keto acid complex]]
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[[Category: dihydrolipoamide dehydrogenase]]
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[[Category: Dihydrolipoamide dehydrogenase]]
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[[Category: dihydrolipoamide dehydrogenase binding protein]]
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[[Category: Dihydrolipoamide dehydrogenase binding protein]]
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[[Category: dihydrolipoyl dehydrogenase]]
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[[Category: Dihydrolipoyl dehydrogenase]]
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[[Category: e3]]
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[[Category: E3]]
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[[Category: e3-binding protein]]
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[[Category: E3-binding protein]]
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[[Category: flavin adenine dinucleotide cofactor]]
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[[Category: Flavin adenine dinucleotide cofactor]]
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[[Category: human]]
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[[Category: Human]]
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[[Category: pyruvate dehydrogenase complex]]
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[[Category: Pyruvate dehydrogenase complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:13:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:43:11 2008''
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Revision as of 15:13, 3 May 2008

Image:1zy8.gif

Template:STRUCTURE 1zy8

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


Overview

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.

About this Structure

1ZY8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 18:13:41 2008

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