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2ix4

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Revision as of 07:21, 24 July 2019

Arabidopsis thaliana mitochondrial beta-ketoacyl ACP synthase hexanoic acid complex

Structural highlights

2ix4 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1w0i, 2iwy, 2iwz
Activity:	[acyl-carrier-protein_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number 2.3.1.41
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KASM_ARATH] Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ewald R, Kolukisaoglu U, Bauwe U, Mikkat S, Bauwe H. Mitochondrial protein lipoylation does not exclusively depend on the mtKAS pathway of de novo fatty acid synthesis in Arabidopsis. Plant Physiol. 2007 Sep;145(1):41-8. Epub 2007 Jul 6. PMID:17616510 doi:http://dx.doi.org/10.1104/pp.107.104000
↑ Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A. Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase. Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430 doi:http://dx.doi.org/16/2/261

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ix4"

@@ Line 1: / Line 1: @@
 ==Arabidopsis thaliana mitochondrial beta-ketoacyl ACP synthase hexanoic acid complex==
-<StructureSection load='2ix4' size='340' side='right' caption='[[2ix4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='2ix4' size='340' side='right'caption='[[2ix4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2ix4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IX4 FirstGlance]. <br>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 2ix4" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Arath]]
+[[Category: Large Structures]]
 [[Category: Christensen, C E]]
 [[Category: Henriksen, A]]

2ix4

From Proteopedia

Revision as of 07:21, 24 July 2019

Arabidopsis thaliana mitochondrial beta-ketoacyl ACP synthase hexanoic acid complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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