2le3: Difference between revisions
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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 | <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 [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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 == | ||
| Line 15: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2le3" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 22: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rao JN]] | ||
[[Category: | [[Category: Ulmer TS]] | ||
Latest revision as of 08:42, 15 May 2024
N-terminal regulatory segment of carnitine palmitoyltransferase 1AN-terminal regulatory segment of carnitine palmitoyltransferase 1A
Structural highlights
FunctionPublication 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
|
| ||||||||||||||||