2vig: Difference between revisions

Latest revision as of 15:21, 13 December 2023

Crystal structure of human short-chain acyl CoA dehydrogenase

Structural highlights

2vig is a 8 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 1.9Å
Ligands:	COS, EDO, FAD
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACADS_HUMAN Short chain acyl-CoA dehydrogenase deficiency. The disease is caused by variants affecting the gene represented in this entry.

Function

ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486).[UniProtKB:P15651]^[1] ^[2]

Evolutionary Conservation

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

References

↑ Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N. Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. PMID:11134486 doi:10.1203/00006450-200101000-00008
↑ He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab. 2011 Apr;102(4):418-29. PMID:21237683 doi:10.1016/j.ymgme.2010.12.005

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Corydon MJ, Vockley J, Rinaldo P, Rhead WJ, Kjeldsen M, Winter V, Riggs C, Babovic-Vuksanovic D, Smeitink J, De Jong J, Levy H, Sewell AC, Roe C, Matern D, Dasouki M, Gregersen N. Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res. 2001 Jan;49(1):18-23. PMID:11134486 doi:10.1203/00006450-200101000-00008

[2] He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J. Identification and characterization of new long chain acyl-CoA dehydrogenases. Mol Genet Metab. 2011 Apr;102(4):418-29. PMID:21237683 doi:10.1016/j.ymgme.2010.12.005

[1]

[2]

@@ Line 1: / Line 1: @@
-[[Image:2vig.jpg|left|200px]]
-<!--
+==Crystal structure of human short-chain acyl CoA dehydrogenase==
-The line below this paragraph, containing "STRUCTURE_2vig", creates the "Structure Box" on the page.
+<StructureSection load='2vig' size='340' side='right'caption='[[2vig]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2vig]] is a 8 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=2VIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VIG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-{{STRUCTURE_2vig|  PDB=2vig  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [https://pdbe.org/2vig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB], [https://www.ebi.ac.uk/pdbsum/2vig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vig ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ACADS_HUMAN ACADS_HUMAN] Short chain acyl-CoA dehydrogenase deficiency. The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/ACADS_HUMAN ACADS_HUMAN] Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains (PubMed:21237683, PubMed:11134486).[UniProtKB:P15651]<ref>PMID:11134486</ref> <ref>PMID:21237683</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/vi/2vig_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=2vig ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF HUMAN SHORT-CHAIN ACYL COA DEHYDROGENASE'''
+==See Also==
+*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-VIG is a [[Single protein]] structure of 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=2VIG OCA].
+__TOC__
-[[Category: Butyryl-CoA dehydrogenase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Arrowsmith CH]]
-[[Category: Delft, F Von.]]
+[[Category: Edwards A]]
-[[Category: Edwards, A.]]
+[[Category: Gileadi O]]
-[[Category: Gileadi, O.]]
+[[Category: Oppermann U]]
-[[Category: Oppermann, U.]]
+[[Category: Pantic N]]
-[[Category: Pantic, N.]]
+[[Category: Parizotto E]]
-[[Category: Parizotto, E.]]
+[[Category: Pike ACW]]
-[[Category: Pike, A C.W.]]
+[[Category: Ugochukwu E]]
-[[Category: Ugochukwu, E.]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J.]]
+[[Category: Von Delft F]]
-[[Category: Beta oxidation]]
-[[Category: Disease mutation]]
-[[Category: Fad]]
-[[Category: Fatty acid metabolism]]
-[[Category: Flavoprotein]]
-[[Category: Lipid metabolism]]
-[[Category: Mitochondrion]]
-[[Category: Oxidoreductase]]
-[[Category: Polymorphism]]
-[[Category: Transit peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:51:53 2008''

2vig: Difference between revisions

Latest revision as of 15:21, 13 December 2023

Crystal structure of human short-chain acyl CoA dehydrogenase

Structural highlights

Disease

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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