9ngm: Difference between revisions

Latest revision as of 13:04, 17 December 2025

CryoEM structure of human ABCD3

Structural highlights

9ngm is a 2 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:	Electron Microscopy, Resolution 3.33Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ABCD3_HUMAN The disease is caused by variants affecting the gene represented in this entry.

Function

ABCD3_HUMAN Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation (PubMed:11248239, PubMed:24333844, PubMed:25168382, PubMed:29397936). Has fatty acyl-CoA thioesterase and ATPase activities (PubMed:29397936). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation (PubMed:24333844, PubMed:25944712).[UniProtKB:P33897]^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Roerig P, Mayerhofer P, Holzinger A, Gartner J. Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters. FEBS Lett. 2001 Mar 9;492(1-2):66-72. doi: 10.1016/s0014-5793(01)02235-9. PMID:11248239 doi:https://dx.doi.org/10.1016/s0014-5793(01)02235-9
↑ van Roermund CW, Ijlst L, Wagemans T, Wanders RJ, Waterham HR. A role for the human peroxisomal half-transporter ABCD3 in the oxidation of dicarboxylic acids. Biochim Biophys Acta. 2014 Apr 4;1841(4):563-8. PMID:24333844 doi:10.1016/j.bbalip.2013.12.001
↑ Ferdinandusse S, Jimenez-Sanchez G, Koster J, Denis S, Van Roermund CW, Silva-Zolezzi I, Moser AB, Visser WF, Gulluoglu M, Durmaz O, Demirkol M, Waterham HR, Gökcay G, Wanders RJ, Valle D. A novel bile acid biosynthesis defect due to a deficiency of peroxisomal ABCD3. Hum Mol Genet. 2015 Jan 15;24(2):361-70. PMID:25168382 doi:10.1093/hmg/ddu448
↑ Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C. N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. PMID:25944712 doi:10.1002/pmic.201400617
↑ Okamoto T, Kawaguchi K, Watanabe S, Agustina R, Ikejima T, Ikeda K, Nakano M, Morita M, Imanaka T. Characterization of human ATP-binding cassette protein subfamily D reconstituted into proteoliposomes. Biochem Biophys Res Commun. 2018 Feb 19;496(4):1122-1127. doi:, 10.1016/j.bbrc.2018.01.153. Epub 2018 Feb 3. PMID:29397936 doi:https://dx.doi.org/10.1016/j.bbrc.2018.01.153

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OCA

[1] Roerig P, Mayerhofer P, Holzinger A, Gartner J. Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters. FEBS Lett. 2001 Mar 9;492(1-2):66-72. doi: 10.1016/s0014-5793(01)02235-9. PMID:11248239 doi:https://dx.doi.org/10.1016/s0014-5793(01)02235-9

[2] van Roermund CW, Ijlst L, Wagemans T, Wanders RJ, Waterham HR. A role for the human peroxisomal half-transporter ABCD3 in the oxidation of dicarboxylic acids. Biochim Biophys Acta. 2014 Apr 4;1841(4):563-8. PMID:24333844 doi:10.1016/j.bbalip.2013.12.001

[3] Ferdinandusse S, Jimenez-Sanchez G, Koster J, Denis S, Van Roermund CW, Silva-Zolezzi I, Moser AB, Visser WF, Gulluoglu M, Durmaz O, Demirkol M, Waterham HR, Gökcay G, Wanders RJ, Valle D. A novel bile acid biosynthesis defect due to a deficiency of peroxisomal ABCD3. Hum Mol Genet. 2015 Jan 15;24(2):361-70. PMID:25168382 doi:10.1093/hmg/ddu448

[4] Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C. N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. PMID:25944712 doi:10.1002/pmic.201400617

[5] Okamoto T, Kawaguchi K, Watanabe S, Agustina R, Ikejima T, Ikeda K, Nakano M, Morita M, Imanaka T. Characterization of human ATP-binding cassette protein subfamily D reconstituted into proteoliposomes. Biochem Biophys Res Commun. 2018 Feb 19;496(4):1122-1127. doi:, 10.1016/j.bbrc.2018.01.153. Epub 2018 Feb 3. PMID:29397936 doi:https://dx.doi.org/10.1016/j.bbrc.2018.01.153

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9ngm is ON HOLD  until Paper Publication
+==CryoEM structure of human ABCD3==
+<StructureSection load='9ngm' size='340' side='right'caption='[[9ngm]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9ngm]] is a 2 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=9NGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9NGM FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.33&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ngm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ngm OCA], [https://pdbe.org/9ngm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ngm RCSB], [https://www.ebi.ac.uk/pdbsum/9ngm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ngm ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ABCD3_HUMAN ABCD3_HUMAN] The disease is caused by variants affecting the gene represented in this entry.
+== Function ==
+[https://www.uniprot.org/uniprot/ABCD3_HUMAN ABCD3_HUMAN] Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation (PubMed:11248239, PubMed:24333844, PubMed:25168382, PubMed:29397936). Has fatty acyl-CoA thioesterase and ATPase activities (PubMed:29397936). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation (PubMed:24333844, PubMed:25944712).[UniProtKB:P33897]<ref>PMID:11248239</ref> <ref>PMID:24333844</ref> <ref>PMID:25168382</ref> <ref>PMID:25944712</ref> <ref>PMID:29397936</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Gupta M]]
+[[Category: Khandelwal NK]]
+[[Category: Stroud RM]]

9ngm: Difference between revisions

Latest revision as of 13:04, 17 December 2025

CryoEM structure of human ABCD3

Structural highlights

Disease

Function

References

Contents

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