2cf2
From Proteopedia
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| - | [[Image:2cf2.gif|left|200px]] | + | [[Image:2cf2.gif|left|200px]] |
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| - | '''ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE''' | + | {{Structure |
| + | |PDB= 2cf2 |SIZE=350|CAPTION= <scene name='initialview01'>2cf2</scene>, resolution 4.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CF2 is a [ | + | 2CF2 is a [[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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF2 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16513975 16513975] |
[[Category: Fatty Acid Synthase]] | [[Category: Fatty Acid Synthase]] | ||
[[Category: Fatty-acid synthase]] | [[Category: Fatty-acid synthase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:32 2008'' |
Revision as of 14:14, 20 March 2008
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| , resolution 4.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Fatty-acid synthase, with EC number 2.3.1.85 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE
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.
About 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]. Full crystallographic information is available from OCA.
Reference
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 Mar 20 16:14:32 2008
