2cf2: Difference between revisions

Revision as of 17:48, 21 February 2008

ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE

OverviewOverview

The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.

About this StructureAbout this Structure

2CF2 is a Single protein structure of sequence from Sus scrofa. The following page contains interesting information on the relation of 2CF2 with [Fatty Acid Synthase]. Active as Fatty-acid synthase, with EC number 2.3.1.85 Full crystallographic information is available from OCA.

ReferenceReference

Architecture of mammalian fatty acid synthase at 4.5 A resolution., Maier T, Jenni S, Ban N, Science. 2006 Mar 3;311(5765):1258-62. PMID:16513975

Page seeded by OCA on Thu Feb 21 16:48:03 2008

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OCA

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-[[Image:2cf2.gif|left|200px]]<br />
+[[Image:2cf2.gif|left|200px]]<br /><applet load="2cf2" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2cf2" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2cf2, resolution 4.30&Aring;" />
 '''ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE'''<br />
 ==Overview==
-The homodimeric mammalian fatty acid synthase is one of the most complex, cellular multienzymes, in that each 270-kilodalton polypeptide chain, carries all seven functional domains required for fatty acid synthesis. We, have calculated a 4.5 angstrom-resolution x-ray crystallographic map of, porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic, domains responsible for the cyclic elongation of fatty acid chains into, the electron density. The positioning of domains reveals the complex, architecture of the multienzyme forming an intertwined dimer with two, lateral semicircular reaction chambers, each containing a full set of, catalytic domains required for fatty acid elongation. Large distances, between active sites and conformational differences between the reaction, chambers demonstrate that mobility of the acyl carrier protein and general, flexibility of the multienzyme must accompany handover of the reaction, intermediates during the reaction cycle.
+The homodimeric mammalian fatty acid synthase is one of the most complex cellular multienzymes, in that each 270-kilodalton polypeptide chain carries all seven functional domains required for fatty acid synthesis. We have calculated a 4.5 angstrom-resolution x-ray crystallographic map of porcine fatty acid synthase, highly homologous to the human multienzyme, and placed homologous template structures of all individual catalytic domains responsible for the cyclic elongation of fatty acid chains into the electron density. The positioning of domains reveals the complex architecture of the multienzyme forming an intertwined dimer with two lateral semicircular reaction chambers, each containing a full set of catalytic domains required for fatty acid elongation. Large distances between active sites and conformational differences between the reaction chambers demonstrate that mobility of the acyl carrier protein and general flexibility of the multienzyme must accompany handover of the reaction intermediates during the reaction cycle.
 ==About this Structure==
-CF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. The following page contains interesting information on the relation of 2CF2 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CF2 OCA].
+CF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. The following page contains interesting information on the relation of 2CF2 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. 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=2CF2 OCA].
 ==Reference==
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 [[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:08:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:03 2008''