5j5z: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5j5z is ~~ON HOLD~~ ~~until Paper Publication~~

==Crystal structure of the D444V disease-causing mutant of the human dihydrolipoamide dehydrogenase==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5j5z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5Z OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5Z FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5z OCA], [http://pdbe.org/5j5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5z RCSB], [http://www.ebi.ac.uk/pdbsum/5j5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5z ProSAT]</td></tr>

</table>

== Disease ==

[[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.

== Function ==

[[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.

__TOC__

</StructureSection>

[[Category: Dihydrolipoyl dehydrogenase]]

[[Category: Adam-Vizi, V]]

[[Category: Ambrus, A]]

[[Category: Mizsei, R]]

[[Category: Szabo, E]]

[[Category: Torocsik, B]]

[[Category: Weiss, M S]]

[[Category: Zambo, Z]]

[[Category: Dihydrolipoamide dehydrogenase]]

[[Category: Disease-causing mutant]]

[[Category: E3 deficiency]]

[[Category: E3 subunit]]

[[Category: Oxidoreductase]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5j5z is ON HOLD  until Paper Publication
+==Crystal structure of the D444V disease-causing mutant of the human dihydrolipoamide dehydrogenase==
+<StructureSection load='5j5z' size='340' side='right' caption='[[5j5z]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5j5z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5Z FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=5j5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5z OCA], [http://pdbe.org/5j5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5z RCSB], [http://www.ebi.ac.uk/pdbsum/5j5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5z ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[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.
+== Function ==
+[[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.
+__TOC__
+</StructureSection>
+[[Category: Dihydrolipoyl dehydrogenase]]
+[[Category: Adam-Vizi, V]]
+[[Category: Ambrus, A]]
+[[Category: Mizsei, R]]
+[[Category: Szabo, E]]
+[[Category: Torocsik, B]]
+[[Category: Weiss, M S]]
+[[Category: Zambo, Z]]
+[[Category: Dihydrolipoamide dehydrogenase]]
+[[Category: Disease-causing mutant]]
+[[Category: E3 deficiency]]
+[[Category: E3 subunit]]
+[[Category: Oxidoreductase]]