2png
From Proteopedia
(New page: 200px<br /><applet load="2png" size="450" color="white" frame="true" align="right" spinBox="true" caption="2png" /> '''Type I rat fatty acid synthase acyl carrier ...) |
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'''Type I rat fatty acid synthase acyl carrier protein (ACP) domain'''<br /> | '''Type I rat fatty acid synthase acyl carrier protein (ACP) domain'''<br /> | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2PNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure superseeds the now removed PDB entry 1N8L. Active as [http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] Full crystallographic information is available from [http:// | + | 2PNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure superseeds the now removed PDB entry 1N8L. Active as [http://en.wikipedia.org/wiki/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PNG OCA]. |
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| + | ==Reference== | ||
| + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17971456 17971456] | ||
[[Category: Fatty-acid synthase]] | [[Category: Fatty-acid synthase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 10:42:56 2008'' |
Revision as of 08:42, 23 January 2008
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Type I rat fatty acid synthase acyl carrier protein (ACP) domain
Overview
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.
About this Structure
2PNG is a Single protein structure of sequence from Rattus norvegicus. This structure superseeds the now removed PDB entry 1N8L. Active as Fatty-acid synthase, with EC number 2.3.1.85 Full crystallographic information is available from OCA.
Reference
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
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