2ix4: Difference between revisions
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[[Image:2ix4.jpg|left|200px]]<br /><applet load="2ix4" size=" | [[Image:2ix4.jpg|left|200px]]<br /><applet load="2ix4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ix4, resolution 1.95Å" /> | caption="2ix4, resolution 1.95Å" /> | ||
'''ARABIDOPSIS THALIANA MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE HEXANOIC ACID COMPLEX'''<br /> | '''ARABIDOPSIS THALIANA MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE HEXANOIC ACID COMPLEX'''<br /> | ||
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==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/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] Known structural/functional Site: <scene name='pdbsite=ACA:K Binding Site For Chain B'>ACA</scene>. Full crystallographic information is available from [http:// | 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 <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=6NA:'>6NA</scene> 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] Known structural/functional Site: <scene name='pdbsite=ACA:K+Binding+Site+For+Chain+B'>ACA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transit peptide]] | [[Category: transit peptide]] | ||
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Revision as of 11:39, 3 February 2008
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ARABIDOPSIS THALIANA MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE HEXANOIC ACID COMPLEX
OverviewOverview
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 cytoplasmic FAS. KASes catalyze the C(2) fatty, acid elongation reaction using either a Cys-His-His or Cys-His-Asn, catalytic triad. Three KASes with different substrate specificities, participate in synthesis of the C(16) and C(18) products of prokaryotic, FAS. By comparison, mtKAS carries out all elongation reactions in the, mitochondria. We present the X-ray crystal structures of the, Cys-His-His-containing human mtKAS and its hexanoyl complex plus the, hexanoyl complex of the plant mtKAS from Arabidopsis thaliana. The, structures explain (1) the bimodal (C(6) and C(10)-C(12)) substrate, preferences leading to the C(8) lipoic acid precursor and long chains for, the membranes, respectively, and (2) the low cerulenin sensitivity of the, human enzyme; and (3) reveal two different potential acyl-binding-pocket, extensions. Rearrangements taking place in the active site, including, subtle changes in the water network, indicate a change in cooperativity of, the active-site histidines upon primer binding.
About this StructureAbout this Structure
2IX4 is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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