1rx0: Difference between revisions

Latest revision as of 08:26, 14 February 2024

Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.

Structural highlights

1rx0 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.77Å
Ligands:	2MC, ACY, EDO, FAD
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACAD8_HUMAN Defects in ACAD8 are the cause of isobutyryl-CoA dehydrogenase deficiency (IBDD) [MIM:611283. The symptoms of IBDD generally appear until late in infancy or in childhood and can include poor feeding and growth (failure to thrive), a weakened and enlarged heart (dilated cardiomyopathy), seizures, and low numbers of red blood cells (anemia).^[1] ^[2] ^[3]

Function

ACAD8_HUMAN Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex.^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J. Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. PMID:12359132
↑ Sass JO, Sander S, Zschocke J. Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants. J Inherit Metab Dis. 2004;27(6):741-5. PMID:15505379 doi:5394411
↑ Pedersen CB, Bischoff C, Christensen E, Simonsen H, Lund AM, Young SP, Koeberl DD, Millington DS, Roe CR, Roe DS, Wanders RJ, Ruiter JP, Keppen LD, Stein Q, Knudsen I, Gregersen N, Andresen BS. Variations in IBD (ACAD8) in children with elevated C4-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2006 Sep;60(3):315-20. Epub 2006 Jul 20. PMID:16857760 doi:10.1203/01.pdr.0000233085.72522.04
↑ Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F. Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. PMID:11013134 doi:10.1086/303105
↑ Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J. Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. PMID:12359132

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J. Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. PMID:12359132

[2] Sass JO, Sander S, Zschocke J. Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants. J Inherit Metab Dis. 2004;27(6):741-5. PMID:15505379 doi:5394411

[3] Pedersen CB, Bischoff C, Christensen E, Simonsen H, Lund AM, Young SP, Koeberl DD, Millington DS, Roe CR, Roe DS, Wanders RJ, Ruiter JP, Keppen LD, Stein Q, Knudsen I, Gregersen N, Andresen BS. Variations in IBD (ACAD8) in children with elevated C4-carnitine detected by tandem mass spectrometry newborn screening. Pediatr Res. 2006 Sep;60(3):315-20. Epub 2006 Jul 20. PMID:16857760 doi:10.1203/01.pdr.0000233085.72522.04

[4] Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F. Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism. Am J Hum Genet. 2000 Nov;67(5):1095-103. Epub 2000 Sep 29. PMID:11013134 doi:10.1086/303105

[5] Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J. Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. Mol Genet Metab. 2002 Sep-Oct;77(1-2):68-79. PMID:12359132

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1rx0|  PDB=1rx0  |  SCENE=  }}
-===Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.===
-{{ABSTRACT_PUBMED_14752098}}
-==Disease==
+==Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.==
-[[http://www.uniprot.org/uniprot/ACAD8_HUMAN ACAD8_HUMAN]] Defects in ACAD8 are the cause of isobutyryl-CoA dehydrogenase deficiency (IBDD) [MIM:[http://omim.org/entry/611283 611283]]. The symptoms of IBDD generally appear until late in infancy or in childhood and can include poor feeding and growth (failure to thrive), a weakened and enlarged heart (dilated cardiomyopathy), seizures, and low numbers of red blood cells (anemia).<ref>PMID:12359132</ref><ref>PMID:15505379</ref><ref>PMID:16857760</ref>
+<StructureSection load='1rx0' size='340' side='right'caption='[[1rx0]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rx0]] is a 4 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=1RX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RX0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MC:METHACRYLYL-COENZYME+A'>2MC</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1rx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rx0 OCA], [https://pdbe.org/1rx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1rx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rx0 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ACAD8_HUMAN ACAD8_HUMAN] Defects in ACAD8 are the cause of isobutyryl-CoA dehydrogenase deficiency (IBDD) [MIM:[https://omim.org/entry/611283 611283]. The symptoms of IBDD generally appear until late in infancy or in childhood and can include poor feeding and growth (failure to thrive), a weakened and enlarged heart (dilated cardiomyopathy), seizures, and low numbers of red blood cells (anemia).<ref>PMID:12359132</ref> <ref>PMID:15505379</ref> <ref>PMID:16857760</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ACAD8_HUMAN ACAD8_HUMAN] Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex.<ref>PMID:11013134</ref> <ref>PMID:12359132</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rx/1rx0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1rx0 ConSurf].
+<div style="clear:both"></div>
-==Function==
+==See Also==
-[[http://www.uniprot.org/uniprot/ACAD8_HUMAN ACAD8_HUMAN]] Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex.<ref>PMID:11013134</ref><ref>PMID:12359132</ref>
+*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-[[1rx0]] is a 4 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=1RX0 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:014752098</ref><references group="xtra"/><references/>
 [[Category: Homo sapiens]]
-[[Category: Battaile, K P.]]
+[[Category: Large Structures]]
-[[Category: Kim, J J.]]
+[[Category: Battaile KP]]
-[[Category: Nguyen, T V.]]
+[[Category: Kim JJ]]
-[[Category: Vockley, J.]]
+[[Category: Nguyen TV]]
-[[Category: Coenzyme some]]
+[[Category: Vockley J]]
-[[Category: Dehydrogenase]]
-[[Category: Flavoprotein]]
-[[Category: Oxidoreductase]]

1rx0: Difference between revisions

Latest revision as of 08:26, 14 February 2024

Crystal structure of isobutyryl-CoA dehydrogenase complexed with substrate/ligand.

Structural highlights

Disease

Function

Evolutionary Conservation

See Also

References

Contents

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