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

Geethanandan, K.; Abhilash, Joseph; Bharath, S.R.; Sadasivan, C.; Haridas, M.

doi:10.1016/j.ijbiomac.2011.08.021

Cited by 14 publications

(6 citation statements)

References 44 publications

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“…Among the 14 closest homologs, we selected the X-ray crystal structures of three representative templates with the PDB codes 1FAT [49], 1BJQ [50] and 3IPV [51] for a multiple sequence-structure alignment with the DORN1 lectin domain sequence. These templates share significant sequence identity and similarity, low structural resolution and high global sequence coverage over the other L-type lectin homologs (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Computational Analysis of the Ligand Binding Site of the Extracellular ATP Receptor, DORN1

et al. 2016

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DORN1 (also known as P2K1) is a plant receptor for extracellular ATP, which belongs to a large gene family of legume-type (L-type) lectin receptor kinases. Extracellular ATP binds to DORN1 with strong affinity through its lectin domain, and the binding triggers a variety of intracellular activities in response to biotic and abiotic stresses. However, information on the tertiary structure of the ligand binding site of DORN1is lacking, which hampers efforts to fully elucidate the mechanism of receptor action. Available data of the crystal structures from more than 50 L-type lectins enable us to perform an in silico study of molecular interaction between DORN1 and ATP. In this study, we employed a computational approach to develop a tertiary structure model of the DORN1 lectin domain. A blind docking analysis demonstrated that ATP binds to a cavity made by four loops (defined as loops A B, C and D) of the DORN1 lectin domain with high affinity. In silico target docking of ATP to the DORN1 binding site predicted interaction with 12 residues, located on the four loops, via hydrogen bonds and hydrophobic interactions. The ATP binding pocket is structurally similar in location to the carbohydrate binding pocket of the canonical L-type lectins. However, four of the residues predicted to interact with ATP are not conserved between DORN1 and the other carbohydrate-binding lectins, suggesting that diversifying selection acting on these key residues may have led to the ATP binding activity of DORN1. The in silico model was validated by in vitro ATP binding assays using the purified extracellular lectin domain of wild-type DORN1, as well as mutated DORN1 lacking key ATP binding residues.

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Section: Resultsmentioning

confidence: 99%

Computational Analysis of the Ligand Binding Site of the Extracellular ATP Receptor, DORN1

et al. 2016

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“…The dialyzed precipitate was loaded to a 20 9 1.5 cm Superdex G-200 column (GE Healthcare Life Science, Bangalore, India) pre-equilibrated with 0.2 M phosphate buffer (pH 6.9) and eluted with the same buffer containing 0.5 M NaCl. A total of 30 fractions were collected and those exhibiting and amylotic activity (fractions 19,20,21) were pooled together.…”

Section: Methodsmentioning

confidence: 99%

“…Spatholobus parviflorus seed lectin (SPL) belongs to the leguminous lectin family. Structure of the SPL has been solved by Geethanandan et al (19). SPL appears during seed development and remains as such in full-grown seeds (20,21).…”

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confidence: 99%

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A Lectin from Spatholobus parviflorus Inhibits Aspergillus flavus α‐Amylase: Enzyme Kinetics and Thermodynamic Studies

et al. 2014

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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. In this study, it was found that Spatholobus parviflorus seed lectin (SPL) can inhibit the growth of A. flavus with a MIC value of 1.5 mg/mL. The enzyme kinetics, molecular modeling and isothermal titration calorimetric studies suggest that SPL can inhibit α-amylase with Ki value of 0.0042 mm. Hence, it is suggested that the antifungal activity of SPL might be partly due to its ability to inhibit the enzyme α-amylase.

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“…It is probable that the binding of Ca 2+ to the specific domain for the cation changes the tertiary structure of the domain defined as site for the sugar binding and, for the same reason, the structure of the catalytic site for arginine. The ability to bind both cations together in order to develop their binding capacity to specific galactose ligands has been demonstrated for other lectins, such as that purified and crystallized from Spatholobus parviflorus [26].…”

Section: Receptorsmentioning

confidence: 99%

Role of the Cytoskeletal Actomyosin Complex in the Motility of Cyanobacteria and Fungal Spores

Sánchez-Elordi¹,

Díaz²,

Vicente³

et al. 2020

Parasitology and Microbiology Research

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This study demonstrates the involvement of the cytoskeleton in the movement of cyanobacteria and fungal spores to their hosts to establish a state of symbiosis or pathogenicity. The term symbiosis sensu lato is referred not only to commensalism and mutualism but also to the parasitic aberrations. The establishment of association implies that the endohabitant can move on a wet surface until finding an entry point in the exohabitant surface. In aqueous media, the exohabitant secretes glycoproteins that form a chemoattraction gradient for the invading cells. In lichens, the gradient consists of fungal lectins whose function is to recognize a compatible green alga or cyanobacterium. In the case of pathogens, the secreted proteins usually are a mixture that includes false quorum and chemoattractant signals, and cell wall digestive enzymes. The results indicate that fungal lectins and defense proteins bind to specific cell wall receptors for signaling the activation of cytoskeleton, causing successive cycles of cell contraction-relaxation that permits the migration of the endohabitant. In this study, different biochemical and microscopy techniques have been used. The mechanisms through which the cytoskeleton carries out these cycles of cell contractionrelaxation are described, being this a remarkable advance compared to previous results.

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

Cited by 14 publications

References 44 publications

Computational Analysis of the Ligand Binding Site of the Extracellular ATP Receptor, DORN1

Computational Analysis of the Ligand Binding Site of the Extracellular ATP Receptor, DORN1

A Lectin from Spatholobus parviflorus Inhibits Aspergillus flavus α‐Amylase: Enzyme Kinetics and Thermodynamic Studies

Role of the Cytoskeletal Actomyosin Complex in the Motility of Cyanobacteria and Fungal Spores

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