Browse
Submit Data
Databases
API
Help

Dataset Information

31 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14).

ABSTRACT: Mouse vas deferens protein/aldo-keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray diffraction data set was collected to 1.86 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.66, b = 69.14, c = 72.27 A, beta = 96.4 degrees. This is the first crystallization report of a rodent AKR1B7 orthologue.

SUBMITTER: Chung R

PROVIDER: S-EPMC2664770 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Crystallization and preliminary X-ray analysis of a rat aldose reductase-like protein (AKR1B14).

Chung Roland R Endo Satoshi S Hara Akira A El-Kabbani Ossama O

Acta crystallographica. Section F, Structural biology and crystallization communications 20090325 Pt 4

Mouse vas deferens protein/aldo-keto reductase 1B7 (AKR1B7) is involved in the detoxification of isocaproaldehyde, a steroidogenesis byproduct, and of 4-hydroxynonenal formed by lipid peroxidation. The rat orthologue of AKR1B7 has recently been named AKR1B14 in the AKR superfamily. Recombinant AKR1B14 was expressed in a bacterial system and purified to homogeneity. The purified protein was crystallized from polyethylene glycol solutions using the hanging-drop vapour-diffusion method and an X-ray ...[more]

PMID: 19342790

Similar Datasets

Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase.

Project description:Maize aldose reductase (AR) is a member of the aldo-keto reductase superfamily. In contrast to human AR, maize AR seems to prefer the conversion of sorbitol into glucose. The apoenzyme was crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 47.2, b = 54.5, c = 100.6 A and one molecule in the asymmetric unit. Synchrotron X-ray diffraction data were collected and a final resolution limit of 2.0 A was obtained after data reduction. Phasing was carried out by an automated molecular-replacement procedure and structural refinement is currently in progress. The refined structure is expected to shed light on the functional/enzymatic mechanism and the unusual activities of maize AR.

| S-EPMC2339750 | biostudies-literature

Crystallization and preliminary X-ray diffraction analysis of rat protein tyrosine phosphatase eta.

Project description:The rat protein tyrosine phosphatase eta (rPTPeta) is a cysteine-dependent phosphatase which hydrolyzes phosphoester bonds in proteins and other molecules. rPTPeta and its human homologue DEP-1 are involved in neoplastic transformations. Thus, expression of the protein is reduced in all oncogene-transformed thyroid cell lines and is absent in highly malignant thyroid cells. Moreover, consistent with the suggested tumour suppression role of PTPeta, inhibition of the tumorigenic process occurs after its exogenous reconstitution, suggesting that PTPeta might be important for gene therapy of cancers. In this study, the catalytic domain of rPTPeta was produced in Escherichia coli in soluble form and purified to homogeneity. Crystals were obtained by the hanging-drop vapour-diffusion method. Diffraction data were collected to 1.87 A resolution. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.46, b = 63.07, c = 111.64 A, and contains one molecule per asymmetric unit.

| S-EPMC2242866 | biostudies-literature

Crystallization and preliminary X-ray analysis of rat SHPS-1.

Project description:SHPS-1, a receptor-type transmembrane protein, is abundantly expressed in neural and myeloid tissues. The most amino-terminal immunoglobulin-like domain of SHPS-1 plays an important role in a variety of cell functions by binding its ligand CD47. Interaction between SHPS-1 and CD47 is thought to be involved in negative regulation of phagocytosis. The ligand-binding domain of rat SHPS-1 was purified and crystallized using the vapour-diffusion method with the solution-stirring technique. Preliminary X-ray diffraction data were collected from SHPS-1 crystals to 2.8 A resolution and reduced to primitive hexagonal space group P622. Unit-cell parameters are a = b = 100.5, c = 101.3 A.

| S-EPMC2197194 | biostudies-literature

Crystallization and preliminary X-ray diffraction analysis of rat autotaxin.

Project description:Rat autotaxin has been cloned, expressed, purified to homogeneity and crystallized via hanging-drop vapour diffusion using PEG 3350 as precipitant and ammonium iodide and sodium thiocyanate as salts. The crystals diffracted to a maximum resolution of 2.05 A and belonged to space group P1, with unit-cell parameters a=53.8, b=63.3, c=70.5 A, alpha=98.8, beta=106.2, gamma=99.8 degrees. Preliminary X-ray diffraction analysis indicated the presence of one molecule per asymmetric unit, with a solvent content of 47%.

| S-EPMC2935245 | biostudies-literature

Crystallization and preliminary X-ray crystallographic analysis of Sulfolobus solfataricus thioredoxin reductase.

Project description:A thermostable thioredoxin reductase isolated from Sulfolobus solfataricus (SsTrxR) has been successfully crystallized in the absence and in the presence of NADP. Two different crystal forms have been obtained. Crystals of the form that yields higher resolution data (1.8 A) belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.77, b = 120.68, c = 126.85 A. The structure of the enzyme has been solved by MAD methods using the anomalous signal from the Se atoms of selenomethionine-labelled SsTrxR.

| S-EPMC1991316 | biostudies-literature

Crystallization and preliminary X-ray analysis of enoyl-acyl carrier protein reductase (FabK) from Streptococcus pneumoniae.

Project description:The enoyl-acyl carrier protein (ACP) reductase from Streptococcus pneumoniae (FabK; EC 1.3.1.9) is responsible for catalyzing the final step in each elongation cycle of fatty-acid biosynthesis. Selenomethionine-substituted FabK was purified and crystallized by the hanging-drop vapour-diffusion method at 277 K. The crystal belongs to space group P2(1), with unit-cell parameters a = 50.26, b = 126.70, c = 53.63 A, beta = 112.46 degrees . Diffraction data were collected to 2.00 A resolution using synchrotron beamline BL32B2 at SPring-8. Two molecules were estimated to be present in the asymmetric unit, with a solvent content of 45.1%.

| S-EPMC2243098 | biostudies-literature

Crystallization and preliminary X-ray diffraction analysis of the putative aldose 1-epimerase YeaD from Escherichia coli.

Project description:Escherichia coli YeaD (ecYeaD) is suggested to be a member of the galactose mutarotase-like superfamily. Galactose mutarotase is an enzyme that converts alpha-galactose to beta-galactose. The known structures of these galactose mutarotase-like proteins are similar to those of galactose mutarotases, with the catalytic residues being conserved, but there are some differences between them in the substrate-binding pocket. In order to reveal the specificity of ecYeaD, a three-dimensional structure is essential. Full-length ecYeaD with an additional 6xHis tag at the C-terminus was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as a precipitant at 283 K. An X-ray diffraction data set was collected to a resolution of 1.9 A from a single flash-cooled crystal that belonged to space group P2(1)2(1)2(1).

| S-EPMC2917301 | biostudies-literature

Crystallization and preliminary X-ray crystallographic analysis of a carbonyl reductase from Candida parapsilosis.

Project description:A novel short-chain NADPH-dependent (S)-1-phenyl-1,2-ethanediol dehydrogenase (SCR) has been crystallized. Two distinct but related crystal forms of SCR were obtained using the hanging-drop vapour-diffusion method and a reservoir solution consisting of 18%(w/v) polyethylene glycol 2000 monomethyl ether and 8%(v/v) 2-propanol as the precipitant. The crystals were rhomboid in shape with average dimensions of 0.3 x 0.3 x 0.4 mm and diffracted to a resolution of 2.7-3.0 A. The crystal forms both belong to space group P2(1)2(1)2(1) and have unit-cell parameters a = 104.7, b = 142.8, c = 151.8 A and a = 101.1, b = 146.0, c = 159.8 A. The calculated values of V(M), rotation-function and translation-function solutions and consideration of potential crystal packing suggest that there are eight protein subunits per asymmetric unit.

| S-EPMC2374259 | biostudies-literature

Crystallization and preliminary X-ray diffraction analysis of (R)-carbonyl reductase from Candida parapsilosis.

Project description:The NADH-dependent (R)-carbonyl reductase from Candida parapsilosis (RCR) catalyzes the asymmetric reduction of 2-hydroxyacetophenone (HAP) to produce (R)-1-phenyl-1,2-ethanediol [(R)-PED], which is used as a versatile building block for the synthesis of pharmaceuticals and fine chemicals. To gain insight into the catalytic mechanism, the structures of complexes of RCR with ligands, including the coenzyme, are important. Here, the recombinant RCR protein was expressed and purified in Escherichia coli and was crystallized in the presence of NAD+. The crystals, which belonged to the orthorhombic space group P2?2?2?, with unit-cell parameters a=85.64, b=106.11, c=145.55?Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.15?Å resolution. Initial model building indicates that RCR forms a homotetramer, consistent with previous reports of medium-chain-type alcohol dehydrogenases.

| S-EPMC4051541 | biostudies-literature

Purification, crystallization and preliminary X-ray crystallographic analysis of xylose reductase from Candida tropicalis.

Project description:Xylose reductase (XR), which requires NADPH as a co-substrate, catalyzes the reduction of D-xylose to xylitol, which is the first step in the metabolism of D-xylose. The detailed three-dimensional structure of XR will provide a better understanding of the biological significance of XR in the efficient production of xylitol from biomass. XR of molecular mass 36.6 kDa from Candida tropicalis was crystallized using the hanging-drop vapour-diffusion method. According to X-ray diffraction data from C. tropicalis XR crystals at 2.91 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicated the presence of four XR molecules in the asymmetric unit, with 68.0% solvent content.

| S-EPMC2664776 | 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