2le3: Difference between revisions

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[[Image:2le3.png|left|200px]]


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==N-terminal regulatory segment of carnitine palmitoyltransferase 1A==
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<StructureSection load='2le3' size='340' side='right'caption='[[2le3]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
{{STRUCTURE_2le3|  PDB=2le3  |  SCENE=  }}
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== Function ==
[https://www.uniprot.org/uniprot/CPT1A_HUMAN CPT1A_HUMAN]
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== 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.


===N-terminal regulatory segment of carnitine palmitoyltransferase 1A===
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<ref>PMID:21990363</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2le3" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]]
(as it appears on PubMed at http://www.pubmed.gov), where 21990363 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21990363}}
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</StructureSection>
==About this Structure==
[[2le3]] is a 1 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:021990363</ref><references group="xtra"/>
[[Category: Carnitine O-palmitoyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Rao, J N.]]
[[Category: Large Structures]]
[[Category: Ulmer, T S.]]
[[Category: Rao JN]]
[[Category: Amphiphilic structure]]
[[Category: Ulmer TS]]
[[Category: Membrane protein]]
[[Category: Membrane-protein interaction]]
[[Category: Structural switch]]
[[Category: Transferase]]

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