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| | ==N-terminal regulatory segment of carnitine palmitoyltransferase 1A== | | ==N-terminal regulatory segment of carnitine palmitoyltransferase 1A== |
| - | <StructureSection load='2le3' size='340' side='right'caption='[[2le3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2le3' size='340' side='right'caption='[[2le3]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2le3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2le3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LE3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPT1A, CPT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le3 OCA], [https://pdbe.org/2le3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le3 RCSB], [https://www.ebi.ac.uk/pdbsum/2le3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le3 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carnitine_O-palmitoyltransferase Carnitine O-palmitoyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.21 2.3.1.21] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le3 OCA], [https://pdbe.org/2le3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2le3 RCSB], [https://www.ebi.ac.uk/pdbsum/2le3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2le3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CPT1A_HUMAN CPT1A_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Carnitine O-palmitoyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rao, J N]] | + | [[Category: Rao JN]] |
| - | [[Category: Ulmer, T S]] | + | [[Category: Ulmer TS]] |
| - | [[Category: Amphiphilic structure]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Membrane-protein interaction]]
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| - | [[Category: Structural switch]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
CPT1A_HUMAN
Publication Abstract from PubMed
The enzyme carnitine palmitoyltransferase 1 (CPT1), which is anchored in the outer mitochondrial membrane (OMM), controls the rate-limiting step in fatty acid beta-oxidation in mammalian tissues. It is inhibited by malonyl-CoA, the first intermediate of fatty acid synthesis, and it responds to OMM curvature and lipid characteristics, which reflect long term nutrient/hormone availability. Here, we show that the N-terminal regulatory domain (N) of CPT1A can adopt two complex amphiphilic structural states, termed Nalpha and Nbeta, that interchange in a switch-like manner in response to offered binding surface curvature. Structure-based site-directed mutageneses of native CPT1A suggest Nalpha to be inhibitory and Nbeta to be noninhibitory, with the relative Nalpha/Nbeta ratio setting the prevalent malonyl-CoA sensitivity of the enzyme. Based on the amphiphilic nature of N and molecular modeling, we propose malonyl-CoA sensitivity to be coupled to the properties of the OMM by Nalpha-OMM associations that alter the Nalpha/Nbeta ratio. For enzymes residing at the membrane-water interface, this constitutes an integrative regulatory mechanism of exceptional sophistication.
An Environment-dependent Structural Switch Underlies the Regulation of Carnitine Palmitoyltransferase 1A.,Rao JN, Warren GZ, Estolt-Povedano S, Zammit VA, Ulmer TS J Biol Chem. 2011 Dec 9;286(49):42545-54. Epub 2011 Oct 11. PMID:21990363[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rao JN, Warren GZ, Estolt-Povedano S, Zammit VA, Ulmer TS. An Environment-dependent Structural Switch Underlies the Regulation of Carnitine Palmitoyltransferase 1A. J Biol Chem. 2011 Dec 9;286(49):42545-54. Epub 2011 Oct 11. PMID:21990363 doi:10.1074/jbc.M111.306951
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