A profile of protein-protein interaction: Crystal structure of a lectin-lectin complex.

Proteins may utilize complex networks of interactions to create/proceed signaling pathways of highly adaptive responses such as programmed cell death. Direct binary interactions study of proteins may help propose models for protein-protein interaction. Towards this goal we applied a combination of thermodynamic kinetics and crystal structure analyses to elucidate the complexity and diversity in such interactions.

Xylanase and cellulase systems of Clostridium sp.: an insight on molecular approaches for strain improvement.

Bioethanol and biobutanol hold great promise as alternative biofuels, especially for transport sector, because they can be produced from lignocellulosic agro-industrial residues. From techno-economic point of view, the bioprocess for biofuels production should involve minimal processing steps. Consolidated bioprocessing (CBP), which combines various processing steps such as pretreatment, hydrolysis and fermentation in a single bioreactor, could be of great relevance for the production of bioethanol and biobutanol or solvents (acetone, butanol, ethanol), employing clostridia.

A lectin from Spatholobus parviflorus inhibits Aspergillus flavus α-amylase: enzyme kinetics and thermodynamic studies.

Aspergillus flavus is a commonly found fungal pathogen which produces structurally related and highly toxic secondary metabolites, aflatoxins. It has been proposed that α-amylase inhibitors may limit the ability of the fungus to produce aflatoxins. Hence, this enzyme is a potent target for the development of antifungal agents.

Production, purification, characterization and over-expression of xylanases from actinomycetes.

Xylanases are a group of depolymerizing enzymes often used for the hydrolysis of xylan (present in hemicellulose) to monomeric sugars and comprise endo-xylanases (EC 3.2.1.

Carbohydrate binding and unfolding of Spatholobus parviflorus lectin: fluorescence and circular dichroism spectroscopic study.

Biophysical and carbohydrate binding studies have been carried out on a lectin of Spatholobus parviflorus (SPL) seeds isolated by affinity chromatography on cross-linked guar gum. It agglutinated erythrocytes of all ABO blood groups. SDS-PAGE, both in reducing and non-reducing conditions, showed two bands with MW of 29 and 31 kDa.

Metal ions in sugar binding, sugar specificity and structural stability of Spatholobus parviflorus seed lectin.

Spatholobus parviflorus seed lectin (SPL) is a heterotetrameric lectin, with two α and two β monomers. In the crystal structure of SPL α monomer, two residues at positions 240 and 241 are missing. This region was modeled based on the positional and sequence similarities.

Inverted binding due to a minor structural change in berberine enhances its phospholipase A2 inhibitory effect.

Biotransformation of berberine by Rhizopus oryzae leads to its demethylation, producing hydroxyl derivatives, as revealed by Fourier Transform Infra Red spectroscopy, Nuclear Magnetic Resonance and Electro Spray Ionization-Mass Spectrometric analyses. Surface Plasmon Resonance and enzyme kinetic studies showed that biotransformed derivatives of berberine had a higher inhibitory potential than berberine towards phospholipase A(2). X-ray crystal structures demonstrated that biotransformed berberine binds to PLA(2) in an entirely different, inverted orientation with respect to the binding of berberine.

X-ray structure of a galactose-specific lectin from Spatholobous parviflorous.

A galactose-specific seed lectin from Spatholobous parviflorus (SPL) has been purified, crystallized and its X-ray structure solved. It is the first lectin purified and crystallized from the genus Spatholobus (family: Fabaceae). The crystals belong to the space group P1, with a=60.

Crystallization and preliminary X-ray studies of a galactose-specific lectin from the seeds of Spatholobus parviflorus.

A galactose-specific seed lectin was purified from the legume Spatholobus parviflorus and crystallized using the hanging-drop vapour-diffusion technique. The crystals belonged to space group P1, with unit-cell parameters a = 60.998, b = 60.

Crystallization and preliminary X-ray diffraction analysis of a galactose-specific lectin from the seeds of Butea monosperma.

The galactose-specific lectin from the seeds of Butea monosperma has been crystallized by the hanging-drop vapour-diffusion technique. The crystals belonged to space group P1, with unit-cell parameters a = 78.45, b = 78.