This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1egc

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA

Structural highlights

1egc 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 2.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ACADM_HUMAN Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14] ^[15]

Function

ACADM_HUMAN This enzyme is specific for acyl chain lengths of 4 to 16.

Evolutionary Conservation

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

References

↑ Matsubara Y, Narisawa K, Miyabayashi S, Tada K, Coates PM, Bachmann C, Elsas LJ 2nd, Pollitt RJ, Rhead WJ, Roe CR. Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Biochem Biophys Res Commun. 1990 Aug 31;171(1):498-505. PMID:2393404
↑ Yokota I, Indo Y, Coates PM, Tanaka K. Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. J Clin Invest. 1990 Sep;86(3):1000-3. PMID:2394825 doi:http://dx.doi.org/10.1172/JCI114761
↑ Kelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW. Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9236-40. PMID:2251268
↑ Yokota I, Coates PM, Hale DE, Rinaldo P, Tanaka K. Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. Am J Hum Genet. 1991 Dec;49(6):1280-91. PMID:1684086
↑ Gregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al.. Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. Hum Genet. 1991 Apr;86(6):545-51. PMID:1902818
↑ Blakemore AI, Singleton H, Pollitt RJ, Engel PC, Kolvraa S, Gregersen N, Curtis D. Frequency of the G985 MCAD mutation in the general population. Lancet. 1991 Feb 2;337(8736):298-9. PMID:1671131
↑ Andresen BS, Jensen TG, Bross P, Knudsen I, Winter V, Kolvraa S, Bolund L, Ding JH, Chen YT, Van Hove JL, et al.. Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. Am J Hum Genet. 1994 Jun;54(6):975-88. PMID:8198141
↑ Ziadeh R, Hoffman EP, Finegold DN, Hoop RC, Brackett JC, Strauss AW, Naylor EW. Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. Pediatr Res. 1995 May;37(5):675-8. PMID:7603790
↑ Brackett JC, Sims HF, Steiner RD, Nunge M, Zimmerman EM, deMartinville B, Rinaldo P, Slaugh R, Strauss AW. A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. J Clin Invest. 1994 Oct;94(4):1477-83. PMID:7929823 doi:http://dx.doi.org/10.1172/JCI117486
↑ Andresen BS, Bross P, Udvari S, Kirk J, Gray G, Kmoch S, Chamoles N, Knudsen I, Winter V, Wilcken B, Yokota I, Hart K, Packman S, Harpey JP, Saudubray JM, Hale DE, Bolund L, Kolvraa S, Gregersen N. The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet. 1997 May;6(5):695-707. PMID:9158144
↑ Kuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S. Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site. Biochem J. 1999 Jan 15;337 ( Pt 2):225-30. PMID:9882619
↑ Yang BZ, Ding JH, Zhou C, Dimachkie MM, Sweetman L, Dasouki MJ, Wilkinson J, Roe CR. Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. Mol Genet Metab. 2000 Mar;69(3):259-62. PMID:10767181 doi:10.1006/mgme.2000.2978
↑ Andresen BS, Dobrowolski SF, O'Reilly L, Muenzer J, McCandless SE, Frazier DM, Udvari S, Bross P, Knudsen I, Banas R, Chace DH, Engel P, Naylor EW, Gregersen N. Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency. Am J Hum Genet. 2001 Jun;68(6):1408-18. Epub 2001 May 8. PMID:11349232 doi:10.1086/320602
↑ Zschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E. Molecular and functional characterisation of mild MCAD deficiency. Hum Genet. 2001 May;108(5):404-8. PMID:11409868
↑ Albers S, Levy HL, Irons M, Strauss AW, Marsden D. Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency. J Inherit Metab Dis. 2001 Jun;24(3):417-8. PMID:11486912

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1egc"

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1egc|  PDB=1egc  |  SCENE=  }}
-===STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA===
-{{ABSTRACT_PUBMED_8823176}}
-==Disease==
+==STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA==
-[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[http://omim.org/entry/201450 201450]]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref><ref>PMID:2394825</ref><ref>PMID:2251268</ref><ref>PMID:1684086</ref><ref>PMID:1902818</ref><ref>PMID:1671131</ref><ref>PMID:8198141</ref><ref>PMID:7603790</ref><ref>PMID:7929823</ref><ref>PMID:9158144</ref><ref>PMID:9882619</ref><ref>PMID:10767181</ref><ref>PMID:11349232</ref><ref>PMID:11409868</ref><ref>PMID:11486912</ref>
+<StructureSection load='1egc' size='340' side='right'caption='[[1egc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
-==Function==
+<table><tr><td colspan='2'>[[1egc]] 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=1EGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGC FirstGlance]. <br>
-[[http://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN]] This enzyme is specific for acyl chain lengths of 4 to 16.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO8:OCTANOYL-COENZYME+A'>CO8</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
-==About this Structure==
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1egc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egc OCA], [https://pdbe.org/1egc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egc RCSB], [https://www.ebi.ac.uk/pdbsum/1egc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egc ProSAT]</span></td></tr>
-[[1egc]] 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=1EGC OCA].
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] Defects in ACADM are the cause of acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:[https://omim.org/entry/201450 201450]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy.<ref>PMID:2393404</ref> <ref>PMID:2394825</ref> <ref>PMID:2251268</ref> <ref>PMID:1684086</ref> <ref>PMID:1902818</ref> <ref>PMID:1671131</ref> <ref>PMID:8198141</ref> <ref>PMID:7603790</ref> <ref>PMID:7929823</ref> <ref>PMID:9158144</ref> <ref>PMID:9882619</ref> <ref>PMID:10767181</ref> <ref>PMID:11349232</ref> <ref>PMID:11409868</ref> <ref>PMID:11486912</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ACADM_HUMAN ACADM_HUMAN] This enzyme is specific for acyl chain lengths of 4 to 16.
+== 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/eg/1egc_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=1egc ConSurf].
+<div style="clear:both"></div>
 ==See Also==
-*[[Acyl-CoA dehydrogenase|Acyl-CoA dehydrogenase]]
+*[[Acyl-CoA dehydrogenase 3D structures|Acyl-CoA dehydrogenase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:008823176</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Oxidoreductase]]
+[[Category: Large Structures]]
-[[Category: Ghisla, S.]]
+[[Category: Ghisla S]]
-[[Category: Kim, J P.]]
+[[Category: Kim JP]]
-[[Category: Lee, H J.]]
+[[Category: Lee HJ]]
-[[Category: Nandy, A.]]
+[[Category: Nandy A]]
-[[Category: Paschke, R.]]
+[[Category: Paschke R]]
-[[Category: Wang, M.]]
+[[Category: Wang M]]
-[[Category: Acyl-coa dehydrogenase]]
-[[Category: Electron transfer]]
-[[Category: Flavoprotein]]

1egc

From Proteopedia

Current revision

STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA

Structural highlights

Disease

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox