This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2ix4
From Proteopedia
(New page: 200px<br /> <applet load="2ix4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ix4, resolution 1.95Å" /> '''ARABIDOPSIS THALIAN...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2IX4 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with K and 6NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IX4 OCA]]. | + | 2IX4 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]] with K and 6NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41]]. Structure known Active Site: ACA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IX4 OCA]]. |
==Reference== | ==Reference== | ||
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase., Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A, Protein Sci. 2007 Feb;16(2):261-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242430 17242430] | Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase., Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A, Protein Sci. 2007 Feb;16(2):261-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242430 17242430] | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Christensen, C.E.]] | [[Category: Christensen, C.E.]] | ||
| Line 33: | Line 34: | ||
[[Category: transit peptide]] | [[Category: transit peptide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:57:54 2007'' |
Revision as of 10:53, 30 October 2007
|
ARABIDOPSIS THALIANA MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE HEXANOIC ACID COMPLEX
Overview
Two distinct ways of organizing fatty acid biosynthesis exist: the, multifunctional type I fatty acid synthase (FAS) of mammals, fungi, and, lower eukaryotes with activities residing on one or two polypeptides; and, the dissociated type II FAS of prokaryotes, plastids, and mitochondria, with individual activities encoded by discrete genes. The beta-ketoacyl, [ACP] synthase (KAS) moiety of the mitochondrial FAS (mtKAS) is targeted, by the antibiotic cerulenin and possibly by the other antibiotics, inhibiting prokaryotic KASes: thiolactomycin, platensimycin, and the, alpha-methylene butyrolactone, C75. The high degree of structural, similarity between mitochondrial and prokaryotic KASes complicates, development of novel antibiotics targeting prokaryotic KAS without, affecting KAS domains of ... [(full description)]
About this Structure
2IX4 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with K and 6NA as [ligands]. Active as [Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [2.3.1.41]. Structure known Active Site: ACA. Full crystallographic information is available from [OCA].
Reference
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase., Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A, Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430
Page seeded by OCA on Tue Oct 30 12:57:54 2007
Categories: Arabidopsis thaliana | Beta-ketoacyl-acyl-carrier-protein synthase I | Single protein | Christensen, C.E. | Henriksen, A. | Kragelund, B. | Wettstein-Knowles, P.Von. | 6NA | K | Acyl complex | Acyltransferase | Beta-ketoacyl-(acyl carrier protein) synthase | Condensing enzyme | Fatty acid biosynthesis | Fatty acid elongation | Lipid metabolism | Lipid synthesis | Mitochondrion | Synthase | Transferase | Transit peptide
