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4ae7

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Crystal structure of human THEM5

Structural highlights

4ae7 is a 1 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 1.45Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THEM5_HUMAN Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleyl-CoA and other unsaturated long-chain fatty acid-CoA esters. Plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin. Required for normal mitochondrial function.^[1]

Publication Abstract from PubMed

Acyl coenzyme A (acyl-CoA) thioesterases hydrolyze thioester bonds in acyl-CoA metabolites. The majority of mammalian thioesterases are alpha/beta-hydrolases and have been studied extensively. A second class of Hotdog-fold enzymes has been less well described. Here, we present a structural and functional analysis of a new mammalian mitochondrial thioesterase, Them5. Them5 and its paralog, Them4, adopt the classical Hotdog-fold structure and form homodimers in crystals. In vitro, Them5 shows strong thioesterase activity with long-chain acyl-CoAs. Loss of Them5 specifically alters the remodeling process of the mitochondrial phospholipid cardiolipin. Them5(-/-) mice show deregulation of lipid metabolism and the development of fatty liver, exacerbated by a high-fat diet. Consequently, mitochondrial morphology is affected, and functions such as respiration and beta-oxidation are impaired. The novel mitochondrial acyl-CoA thioesterase Them5 has a critical and specific role in the cardiolipin remodeling process, connecting it to the development of fatty liver and related conditions.

Acyl coenzyme a thioesterase them5/acot15 is involved in cardiolipin remodeling and Fatty liver development.,Zhuravleva E, Gut H, Hynx D, Marcellin D, Bleck CK, Genoud C, Cron P, Keusch JJ, Dummler B, Esposti MD, Hemmings BA Mol Cell Biol. 2012 Jul;32(14):2685-97. Epub 2012 May 14. PMID:22586271^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhuravleva E, Gut H, Hynx D, Marcellin D, Bleck CK, Genoud C, Cron P, Keusch JJ, Dummler B, Esposti MD, Hemmings BA. Acyl coenzyme a thioesterase them5/acot15 is involved in cardiolipin remodeling and Fatty liver development. Mol Cell Biol. 2012 Jul;32(14):2685-97. Epub 2012 May 14. PMID:22586271 doi:10.1128/MCB.00312-12
↑ Zhuravleva E, Gut H, Hynx D, Marcellin D, Bleck CK, Genoud C, Cron P, Keusch JJ, Dummler B, Esposti MD, Hemmings BA. Acyl coenzyme a thioesterase them5/acot15 is involved in cardiolipin remodeling and Fatty liver development. Mol Cell Biol. 2012 Jul;32(14):2685-97. Epub 2012 May 14. PMID:22586271 doi:10.1128/MCB.00312-12

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ae7"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human THEM5==
-<StructureSection load='4ae7' size='340' side='right' caption='[[4ae7]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+<StructureSection load='4ae7' size='340' side='right'caption='[[4ae7]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ae7]] is a 1 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=4AE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AE7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ae7]] is a 1 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=4AE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AE7 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ae8|4ae8]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ae7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ae7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ae7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ae7 PDBsum]</span></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=4ae7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ae7 OCA], [https://pdbe.org/4ae7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ae7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ae7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ae7 ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/THEM5_HUMAN THEM5_HUMAN] Has acyl-CoA thioesterase activity towards long-chain (C16 and C18) fatty acyl-CoA substrates, with a preference for linoleyl-CoA and other unsaturated long-chain fatty acid-CoA esters. Plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin. Required for normal mitochondrial function.<ref>PMID:22586271</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ae7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 19: / Line 23: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Bleck, C K.E.]]
+[[Category: Large Structures]]
-[[Category: Cron, P.]]
+[[Category: Bleck CKE]]
-[[Category: Dummler, B.]]
+[[Category: Cron P]]
-[[Category: Esposti, M Degli.]]
+[[Category: Degli Esposti M]]
-[[Category: Genoud, C.]]
+[[Category: Dummler B]]
-[[Category: Gut, H.]]
+[[Category: Genoud C]]
-[[Category: Hemmings, B A.]]
+[[Category: Gut H]]
-[[Category: Hynx, D.]]
+[[Category: Hemmings BA]]
-[[Category: Keusch, J J.]]
+[[Category: Hynx D]]
-[[Category: Marcellin, D.]]
+[[Category: Keusch JJ]]
-[[Category: Zhuravleva, E.]]
+[[Category: Marcellin D]]
-[[Category: Hotdog-fold]]
+[[Category: Zhuravleva E]]
-[[Category: Hydrolase]]

4ae7

From Proteopedia

Current revision

Crystal structure of human THEM5

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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