2le3: Difference between revisions
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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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPT1A, CPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPT1A, CPT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnitine_O-palmitoyltransferase Carnitine O-palmitoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.21 2.3.1.21] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnitine_O-palmitoyltransferase Carnitine O-palmitoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.21 2.3.1.21] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le3 OCA], [http://pdbe.org/2le3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2le3 RCSB], [http://www.ebi.ac.uk/pdbsum/2le3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2le3 OCA], [http://pdbe.org/2le3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2le3 RCSB], [http://www.ebi.ac.uk/pdbsum/2le3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2le3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 22:19, 1 August 2018
N-terminal regulatory segment of carnitine palmitoyltransferase 1AN-terminal regulatory segment of carnitine palmitoyltransferase 1A
Structural highlights
Publication Abstract from PubMedThe 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 AlsoReferences
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