Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Crystallization and preliminary crystallographic analysis of a plant type III polyketide synthase that produces benzalacetone.

ABSTRACT: Benzalacetone synthase (BAS) from Rheum palmatum is a plant-specific type III polyketide synthase that catalyzes the one-step decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the diketide 4-(4-hydroxyphenyl)-but-3-en-2-one. Recombinant BAS expressed in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method. The crystals belong to space group P2(1), with unit-cell parameters a = 54.6, b = 89.6, c = 81.1 A, alpha = gamma = 90.0, beta = 100.5 degrees . Diffraction data were collected to 1.8 A resolution using synchrotron radiation at BL24XU of SPring-8.

SUBMITTER: Morita H

PROVIDER: S-EPMC2374239 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Crystallization and preliminary crystallographic analysis of a plant type III polyketide synthase that produces benzalacetone.

Morita Hiroyuki H Tanio Michikazu M Kondo Shin S Kato Ryohei R Wanibuchi Kiyofumi K Noguchi Hiroshi H Sugio Shigetoshi S Abe Ikuro I Kohno Toshiyuki T

Acta crystallographica. Section F, Structural biology and crystallization communications 20080329 Pt 4

Benzalacetone synthase (BAS) from Rheum palmatum is a plant-specific type III polyketide synthase that catalyzes the one-step decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the diketide 4-(4-hydroxyphenyl)-but-3-en-2-one. Recombinant BAS expressed in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method. The crystals belong to space group P2(1), with unit-cell parameters a = 54.6, b = 89.6, c = 81.1 A, alpha = gamma = 90.0, beta = 100.5 degree ...[more]

PMID: 18391433

Similar Datasets

Crystallization and preliminary crystallographic analysis of a novel plant type III polyketide synthase that produces pentaketide chromone.

Project description:Pentaketide chromone synthase (PCS) from Aloe arborescens is a novel plant-specific type III polyketide synthase that catalyzes the formation of 5,7-dihydroxy-2-methylchromone from five molecules of malonyl-CoA. Recombinant PCS expressed in Escherichia coli was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a = 73.2, b = 88.4, c = 70.0 A, alpha = gamma = 90.0, beta = 95.6 degrees . Diffraction data were collected to 1.6 A resolution using synchrotron radiation at BL24XU of SPring-8.

| S-EPMC2242872 | biostudies-literature

Crystallization and preliminary crystallographic analysis of an octaketide-producing plant type III polyketide synthase.

Project description:Octaketide synthase (OKS) from Aloe arborescens is a plant-specific type III polyketide synthase that produces SEK4 and SEK4b from eight molecules of malonyl-CoA. Recombinant OKS expressed in Escherichia coli was crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to space group I422, with unit-cell parameters a = b = 110.2, c = 281.4 A, alpha = beta = gamma = 90.0 degrees . Diffraction data were collected to 2.6 A resolution using synchrotron radiation at BL24XU of SPring-8.

| S-EPMC2339743 | biostudies-literature

Expression, purification and crystallization of a plant type III polyketide synthase that produces diarylheptanoids.

Project description:Curcuminoid synthase (CUS) from Oryza sativa is a plant-specific type III polyketide synthase that catalyzes the one-pot formation of bisdemethoxycurcumin by the condensation of two molecules of 4-coumaroyl-CoA and one molecule of malonyl-CoA. Recombinant CUS was expressed in Escherichia coli and crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P2(1), with unit-cell parameters a=72.7, b=97.2, c=126.2 A, alpha=gamma=90.0, beta=103.7 degrees. A diffraction data set was collected in-house to 2.5 A resolution.

| S-EPMC2917300 | biostudies-literature

Crystallization and preliminary crystallographic analysis of an acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata.

Project description:Polyketide synthase 1 (PKS1) from Huperzia serrata is a plant-specific type III polyketide synthase that shows an unusually versatile catalytic potential, producing various aromatic tetraketides, including chalcones, benzophenones, phlorogulucinols and acridones. Recombinant H. serrata PKS1 expressed in Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 73.3, b = 85.0, c = 137.7 A, alpha = beta = gamma = 90.0 degrees. Diffraction data were collected to 2.0 A resolution using synchrotron radiation at BL24XU of SPring-8.

| S-EPMC2335141 | biostudies-literature

Expression, purification and crystallization of a fungal type III polyketide synthase that produces the csypyrones.

Project description:CsyB from Aspergillus oryzae is a novel type III polyketide synthase that catalyzes the formation of csypyrone B1 [4-(3-acetyl-4-hydroxy-2-oxo-2H-pyran-6-yl)butyric acid] from fatty acyl-CoA, malonyl-CoA and acetoacetyl-CoA. Recombinant CsyB expressed in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space P2₁, with unit-cell parameters a=70.0, b=104.8, c=73.5 Å, β=114.4°.

| S-EPMC4051524 | biostudies-literature

Purification, crystallization and preliminary crystallographic analysis of human cystathionine ?-synthase.

Project description:Human cystathionine ?-synthase (CBS) is a pyridoxal-5'-phosphate-dependent hemeprotein, whose catalytic activity is regulated by S-adenosylmethionine. CBS catalyzes the ?-replacement reaction of homocysteine (Hcy) with serine to yield cystathionine. CBS is a key regulator of plasma levels of the thrombogenic Hcy and deficiency in CBS is the single most common cause of homocystinuria, an inherited metabolic disorder of sulfur amino acids. The properties of CBS enzymes, such as domain organization, oligomerization degree or regulatory mechanisms, are not conserved across the eukaryotes. The current body of knowledge is insufficient to understand these differences and their impact on CBS function and physiology. To overcome this deficiency, we have addressed the crystallization and preliminary crystallographic analysis of a protein construct (hCBS516-525) that contains the full-length CBS from Homo sapiens (hCBS) and just lacks amino-acid residues 516-525, which are located in a disordered loop. The human enzyme yielded crystals belonging to space group I222, with unit-cell parameters a=124.98, b=136.33, c=169.83?Å and diffracting X-rays to a resolution of 3.0?Å. The crystal structure appears to contain two molecules in the asymmetric unit which presumably correspond to a dimeric form of the enzyme.

| S-EPMC3515372 | biostudies-literature

Crystallization and preliminary crystallographic analysis of cysteine synthase from Entamoeba histolytica.

Project description:Entamoeba histolytica, the causative agent of human amoebiasis, is essentially anaerobic, requiring a small amount of oxygen for growth. It cannot tolerate the higher concentration of oxygen present in human tissues or blood. However, during tissue invasion it is exposed to a higher level of oxygen, leading to oxygen stress. Cysteine, which is a vital thiol in E. histolytica, plays an essential role in its oxygen-defence mechanisms. The major route of cysteine biosynthesis in this parasite is the condensation of O-acetylserine with sulfide by the de novo cysteine-biosynthetic pathway, which involves cysteine synthase (EhCS) as a key enzyme. In this study, EhCS was cloned, expressed in Escherichia coli and purified by affinity and size-exclusion chromatography. The purified protein was crystallized in space group P4(1) with two molecules per asymmetric unit and a complete data set was collected to a resolution of 1.86 A. A molecular-replacement solution was obtained using the Salmonella typhimurium O-acetylserine sulfhydrylase structure as a probe and had a correlation coefficient of 37.7% and an R factor of 48.8%.

| S-EPMC2335080 | biostudies-literature

Kingdom-wide analysis of the evolution of the plant type III polyketide synthase superfamily.

Project description:The emergence of type III polyketide synthases (PKSs) was a prerequisite for the conquest of land by the green lineage. Within the PKS superfamily, chalcone synthases (CHSs) provide the entry point reaction to the flavonoid pathway, while LESS ADHESIVE POLLEN 5 and 6 (LAP5/6) provide constituents of the outer exine pollen wall. To study the deep evolutionary history of this key family, we conducted phylogenomic synteny network and phylogenetic analyses of whole-genome data from 126 species spanning the green lineage including Arabidopsis thaliana, tomato (Solanum lycopersicum), and maize (Zea mays). This study thereby combined study of genomic location and context with changes in gene sequences. We found that the two major clades, CHS and LAP5/6 homologs, evolved early by a segmental duplication event prior to the divergence of Bryophytes and Tracheophytes. We propose that the macroevolution of the type III PKS superfamily is governed by whole-genome duplications and triplications. The combined phylogenetic and synteny analyses in this study provide insights into changes in the genomic location and context that are retained for a longer time scale with more recent functional divergence captured by gene sequence alterations.

| S-EPMC8133574 | biostudies-literature

Crystallization and preliminary crystallographic analysis of the type III secretion translocator chaperone SicA from Salmonella enterica.

Project description:SicA is a member of the class II chaperones in type III secretion systems which bind to the pore-forming translocators in the bacterial cytoplasm and prevent them from premature association and degradation. In this study, SicA from Salmonella enterica serovar Typhimurium was overexpressed, purified and crystallized using PEG 8000 as the precipitant. X-ray diffraction data were collected using synchrotron radiation and processed at 3.5 Å resolution. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 180.4, b = 94.1, c = 131.8 Å, β = 130.9°. There may be eight monomers in the crystallographic asymmetric unit, corresponding to a V(M) of 2.52 Å(3) Da(-1) and a solvent content of 51.1%. This suggests an oligomerization state that differs from those of previously reported type III secretion chaperones.

| S-EPMC3001668 | biostudies-literature

Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase.

Project description:Human acylphosphatase, an 11 kDa enzyme that catalyzes the hydrolysis of carboxyl phosphate bonds, has been studied extensively as a model system for amyloid-fibril formation. However, the structure is still not known of any isoform of human acylphosphatase. Here, the crystallization and preliminary X-ray diffraction data analysis of human common-type acylphosphatase are reported. Crystals of human common-type acylphosphatase have been grown by the sitting-drop vapour-diffusion method at 289 K using polyethylene glycol 4000 as precipitant. Diffraction data were collected to 1.45 A resolution at 100 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.58, b = 47.23, c = 57.26 A.

| S-EPMC2150918 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data