Browse
Submit Data
Databases
API
Help

Dataset Information

15 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Crystallization and preliminary X-ray analysis of a cold-active ?-galactosidase from the psychrotrophic and halotolerant Planococcus sp. L4.

ABSTRACT: ?-Galactosidases catalyze the hydrolysis of a galactosyl moiety from the nonreducing termini of oligosaccharides or from glycosides. A novel GH family 42 cold-active ?-galactosidase identified from the psychrotrophic and halotolerant Planococcus sp. L4 (BgaP) was crystallized and a complete data set was collected from a single frozen crystal on an in-house X-ray source. The crystal diffracted to 2.8?Å resolution and belonged to space group P1, with unit-cell parameters a = 104.29, b = 118.12, c = 121.12?Å, ? = 62.66, ? = 69.48, ? = 70.74°. A likely Matthews coefficient of 2.58?Å(3)?Da(-1) and solvent content of 52.32% suggested the presence of six protein subunits in the asymmetric unit.

SUBMITTER: Zhang L

PROVIDER: S-EPMC3151126 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Crystallization and preliminary X-ray analysis of a cold-active β-galactosidase from the psychrotrophic and halotolerant Planococcus sp. L4.

Zhang Liping L Wang Kui K Mo Zhongxing Z Liu Yuhuan Y Hu Xiaopeng X

Acta crystallographica. Section F, Structural biology and crystallization communications 20110720 Pt 8

β-Galactosidases catalyze the hydrolysis of a galactosyl moiety from the nonreducing termini of oligosaccharides or from glycosides. A novel GH family 42 cold-active β-galactosidase identified from the psychrotrophic and halotolerant Planococcus sp. L4 (BgaP) was crystallized and a complete data set was collected from a single frozen crystal on an in-house X-ray source. The crystal diffracted to 2.8 Å resolution and belonged to space group P1, with unit-cell parameters a = 104.29, b = 118.12, c ...[more]

PMID: 21821893

Similar Datasets

Crystallization and preliminary X-ray diffraction data of ?-galactosidase from Aspergillus niger.

Project description:?-Galactosidase from Aspergillus niger (An-?-Gal), belonging to the family 35 glycoside hydrolases, hydrolyzes the ?-galactosidase linkages in lactose and other galactosides. It is extensively used in industry owing to its high hydrolytic activity and safety. The enzyme has been expressed in yeasts and purified by immobilized metal-ion affinity chromatography for crystallization experiments. The recombinant An-?-Gal, deglycosylated to avoid heterogeneity of the sample, has a molecular mass of 109?kDa. Rod-shaped crystals grew using PEG 3350 as the main precipitant agent. A diffraction data set was collected to 1.8?Å resolution.

| S-EPMC4231858 | biostudies-literature

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human ?-galactosidase.

Project description:?-D-Galactosidase (?-Gal) is an exoglycosidase that cleaves ?-galactosides from glycoproteins, sphingolipids and keratan sulfate. This study reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of human lysosomal ?-Gal. The sitting-drop vapour-diffusion method was used to crystallize ?-Gal in complexes with its product galactose and with the inhibitor 1-deoxygalactonojirimycin. The resulting crystals were isomorphous and belonged to space group P2(1). The crystals of the ?-Gal-galactose and the ?-Gal-inhibitor complexes had unit-cell parameters a = 94.8, b = 116.1, c = 140.3 Å, ? = 92.2° and a = 94.8, b = 116.0, c = 140.3 Å, ? = 92.2°, respectively. Diffraction data were collected to 1.8 Å resolution for both crystals.

| S-EPMC3253840 | biostudies-literature

Crystallization and preliminary X-ray crystallographic analysis of beta-galactosidase from Kluyveromyces lactis.

Project description:Beta-galactosidase from Kluyveromyces lactis catalyses the hydrolysis of the beta-galactosidic linkage in lactose. Owing to its many industrial applications, the biotechnological potential of this enzyme is substantial. This protein has been expressed in yeast and purified for crystallization trials. However, optimization of the best crystallization conditions yielded crystals with poor diffraction quality that precluded further structural studies. Finally, the crystal quality was improved using the streak-seeding technique and a complete diffraction data set was collected at 2.8 A resolution.

| S-EPMC2833041 | biostudies-literature

Crystallization and preliminary X-ray diffraction data of alpha-galactosidase from Saccharomyces cerevisiae.

Project description:Saccharomyces cerevisiae alpha-galactosidase is a highly glycosylated extracellular protein that catalyzes the hydrolysis of alpha-galactosidic linkages in various glucids. Its enzymatic activity is of interest in many food-related industries and has biotechnological applications. Glycosylated and in vitro deglycosylated protein samples were both assayed for crystallization, but only the latter gave good-quality crystals that were suitable for X-ray crystallography. The crystals belonged to space group P42(1)2, with unit-cell parameters a = b = 101.24, c = 111.52 A. A complete diffraction data set was collected to 1.95 A resolution using a synchrotron source.

| S-EPMC2805534 | biostudies-literature

Expression, purification, crystallization and preliminary X-ray crystallographic analysis of tomato β-galactosidase 4.

Project description:Plant β-galactosidases play important roles in carbohydrate-reserve mobilization, cell-wall expansion and degradation, and turnover of signalling molecules during ripening. Tomato β-galactosidase 4 (TBG4) not only has β-galactosidase activity but also has exo-β-(1,4)-galactanase activity, and prefers β-(1,4)-galactans longer than pentamers as its substrates; most other β-galactosidases only have the former activity. Recombinant TBG4 protein expressed in the yeast Pichia pastoris was crystallized by the sitting-drop vapour-diffusion method using PEG 10,000 as a precipitant. The crystals belonged to the orthorhombic space group P212121, with unit-parameters a = 92.82, b = 96.30, c = 159.26 Å, and diffracted to 1.65 Å resolution. Calculation of the Matthews coefficient suggested the presence of two monomers per asymmetric unit (VM = 2.2 Å(3) Da(-1)), with a solvent content of 45%.

| S-EPMC4321468 | biostudies-literature

Crystallization and preliminary X-ray analysis of a novel halotolerant feruloyl esterase identified from a soil metagenomic library.

Project description:Feruloyl esterase cleaves the ester linkage formed between ferulic acid and polysaccharides in plant cell walls and thus has wide potential industrial applications. A novel feruloyl esterase (EstF27) identified from a soil metagenomic library was crystallized and a complete data set was collected from a single cooled crystal using an in-house X-ray source. The crystal diffracted to 2.9?Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 94.35, b = 106.19, c = 188.51?Å, ? = ? = ? = 90.00°. A Matthews coefficient of 2.55?Å(3)?Da(-1), with a corresponding solvent content of 51.84%, suggested the presence of ten protein subunits in the asymmetric unit.

| S-EPMC3388917 | biostudies-literature

Characterization of a psychrotrophic Arthrobacter gene and its cold-active beta-galactosidase.

Project description:Enzymes with high specific activities at low temperatures have potential uses for chemical conversions when low temperatures are required, as in the food industry. Psychrotrophic microorganisms which grow at low temperatures may be a valuable source of cold-active enzymes that have higher activities at low temperatures than enzymes found for mesophilic microorganisms. To find cold-active beta-galactosidases, we isolated and characterized several psychrotrophic microorganisms. One isolate, B7, is an Arthrobacter strain which produces beta-galactosidase when grown in lactose minimal media. Extracts have a specific activity at 30 degrees C of 2 U/mg with o-nitrophenyl-beta-D-galactopyranoside as a substrate. Two isozymes were detected when extracts were subjected to electrophoresis in a nondenaturing polyacrylamide gel and stained for activity with 5-bromo-4-chloro-indolyl-beta-D-galactopyranoside (X-Gal). When chromosomal DNA was prepared and transformed into Escherichia coli, three different genes encoding beta-galactosidase activity were obtained. We have subcloned and sequenced one of these beta-galactosidase genes from the Arthrobacter isolate B7. On the basis of amino acid sequence alignment, the gene was found to have probable catalytic sites homologous to those from the E. coli lacZ gene. The gene encoded a protein of 1,016 amino acids with a predicted molecular mass of 111 kDa. The enzyme was purified and characterized. The beta-galactosidase from isolate B7 has kinetic properties similar to those of the E. coli lacZ beta-galactosidase but has a temperature optimum 20 degrees C lower than that of the E. coli enzyme.

| S-EPMC202017 | biostudies-other

Crystallization and preliminary X-ray analysis of alginate importer from Sphingomonas sp. A1.

Project description:Sphingomonas sp. A1 directly incorporates alginate polysaccharides through a 'superchannel' comprising a pit on the cell surface, alginate-binding proteins in the periplasm and an ABC transporter (alginate importer) in the inner membrane. Alginate importer, consisting of four subunits, AlgM1, AlgM2 and two molecules of AlgS, was crystallized in the presence of the binding protein AlgQ2. Preliminary X-ray analysis showed that the crystal diffracted to 3.3 Å resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 72.5, b = 136.8, c = 273.3 Å, suggesting the presence of one complex in the asymmetric unit.

| S-EPMC3310540 | biostudies-literature

Crystallization and preliminary X-ray diffraction analysis of a cold-adapted catalase from Vibrio salmonicida.

Project description:Catalase (EC 1.11.1.6) catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. Recombinant Vibrio salmonicida catalase (VSC) possesses typical cold-adapted features, with higher catalytic efficiency, lower thermal stability and a lower temperature optimum than its mesophilic counterpart from Proteus mirabilis. Crystals of VSC were produced by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 98.15, b = 217.76, c = 99.28 A, beta = 110.48 degrees. Data were collected to 1.96 A and a molecular-replacement solution was found with eight molecules in the asymmetric unit.

| S-EPMC2150922 | biostudies-literature

Crystallization and preliminary X-ray crystallographic studies of ?-transaminase from Mesorhizobium sp. strain LUK.

Project description:?-Transaminase (?-TA) catalyzes the transamination reaction between ?-aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantiochemically pure ?-amino acids for pharmaceutical purposes. The ?-TA from Mesorhizobium sp. strain LUK (?-TAMs) belongs to a novel class in that it shows ?-transaminase activity with a broad and unique substrate specificity. In this study, ?-TAMs was overexpressed in Escherichia coli with an engineered C-terminal His tag. ?-TAMs was then purified to homogeneity and crystallized at 293?K. X-ray diffraction data were collected to a resolution of 2.5?Å from a crystal that belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 90.91, b = 192.17, c = 52.75?Å.

| S-EPMC3034615 | 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