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4da1

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Crystal structure of branched-chain alpha-ketoacid dehydrogenase phosphatase with Mg (II) ions at the active site

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Retrieved from "http://52.214.119.220/wiki/index.php/4da1"

Categories: Homo sapiens | Large Structures | Brautigam CA | Chuang DT | Chuang JL

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4da1]] is a 1 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=4DA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DA1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.383&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4da1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4da1 OCA], [https://pdbe.org/4da1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4da1 RCSB], [https://www.ebi.ac.uk/pdbsum/4da1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4da1 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/PPM1K_HUMAN PPM1K_HUMAN]] Intermediate maple syrup urine disease.
+[https://www.uniprot.org/uniprot/PPM1K_HUMAN PPM1K_HUMAN] Intermediate maple syrup urine disease.
 == Function ==
-[[https://www.uniprot.org/uniprot/PPM1K_HUMAN PPM1K_HUMAN]] Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.<ref>PMID:17374715</ref>
+[https://www.uniprot.org/uniprot/PPM1K_HUMAN PPM1K_HUMAN] Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.<ref>PMID:17374715</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The branched-chain alpha-ketoacid dehydrogenase phosphatase (BDP) component of the human branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) has been expressed in Escherichia coli and purified in the soluble form. The monomeric BDP shows a strict dependence on Mn(2+) ions for phosphatase activity, whereas Mg(2+) and Ca(2+) ions do not support catalysis. Metal binding constants for BDP, determined by competition isothermal titration calorimetry, are 2.4 nm and 10 mum for Mn(2+) and Mg(2+) ions, respectively. Using the phosphorylated decarboxylase component (p-E1b) of BCKDC as a substrate, BDP shows a specific activity of 68 nmol/min/mg. The Ca(2+)-independent binding of BDP to the 24-meric transacylase (dihydrolipoyl transacylase; E2b) core of BCKDC results in a 3-fold increase in the dephosphorylation rate of p-E1b. However, the lipoyl prosthetic group on E2b is not essential for BDP binding or E2b-stimulated phosphatase activity. Acidic residues in the C-terminal linker of the E2b lipoyl domain are essential for the interaction between BDP and E2b. The BDP structure was determined by x-ray crystallography to 2.4 A resolution. The BDP structure is dominated by a central beta-sandwich. There are two protrusions forming a narrow cleft approximately 10 A wide, which constitutes the active site. The carboxylate moieties of acidic residues Asp-109, Asp-207, Asp-298, and Asp-337 in the active-site cleft participate in binding two metal ions. Substitutions of these residues with alanine nullify BDP phosphatase activity. Alteration of the nearby Arg-104 increases the K(m) for p-E1b peptide by 60-fold, suggesting that this residue is critical for the recognition of the native p-E1b protein.
-Structural and biochemical characterization of human mitochondrial branched-chain alpha-ketoacid dehydrogenase phosphatase.,Wynn RM, Li J, Brautigam CA, Chuang JL, Chuang DT J Biol Chem. 2012 Mar 16;287(12):9178-92. Epub 2012 Jan 30. PMID:22291014<ref>PMID:22291014</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4da1" style="background-color:#fffaf0;"></div>
 ==See Also==

4da1

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Current revision

Crystal structure of branched-chain alpha-ketoacid dehydrogenase phosphatase with Mg (II) ions at the active site

Structural highlights

Disease

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