2png

<StructureSection load='2png' size='340' side='right'caption='[[2png]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2png]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n8l 1n8l]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PNG FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8l|1n8l]]</div></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=2png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2png OCA], [https://pdbe.org/2png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2png RCSB], [https://www.ebi.ac.uk/pdbsum/2png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2png ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/FAS_RAT FAS_RAT]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.

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== Publication Abstract from PubMed ==

The synthases that produce fatty acids in mammals (FASs) are arranged as large multidomain polypeptides. The growing fatty acid chain is bound covalently during chain elongation and reduction to the acyl carrier protein (ACP) domain that is then able to access each catalytic site. In this work we report the high-resolution nuclear magnetic resonance (NMR) solution structure of the isolated rat fatty acid synthase apoACP domain. The final ensemble of NMR structures and backbone (15)N relaxation studies show that apoACP adopts a single, well defined fold. On conversion to the holo form, several small chemical shift changes are observed on the ACP for residues surrounding the phosphopantetheine attachment site (as monitored by backbone (1)H-(15)N correlation experiments). However, there are negligible chemical shift changes when the holo form is modified to either the hexanoyl or palmitoyl forms. For further NMR analysis, a (13)C,(15)N-labeled hexanoyl-ACP sample was prepared and full chemical shift assignments completed. Analysis of two-dimensional F(2)-filtered and three-dimensional (13)C-edited nuclear Overhauser effect spectroscopy experiments revealed no detectable NOEs to the acyl chain. These experiments demonstrate that unlike other FAS ACPs studied, this Type I ACP does not sequester a covalently linked acyl moiety, although transient interactions cannot be ruled out. This is an important mechanistic difference between the ACPs from Type I and Type II FASs and may be significant for the modulation and regulation of these important mega-synthases.

A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains.,Ploskon E, Arthur CJ, Evans SE, Williams C, Crosby J, Simpson TJ, Crump MP J Biol Chem. 2008 Jan 4;283(1):518-28. Epub 2007 Oct 30. PMID:17971456<ref>PMID:17971456</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 2png" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Fatty-acid synthase]]

[[Category: Arthur, C J]]

[[Category: Crosby, J]]

[[Category: Crump, M P]]

[[Category: Evans, S E]]

[[Category: Ploskon, E A]]

[[Category: Williams, C]]

[[Category: Transferase]]