7umj | pdb_00007umj

Crystal structure of recombinant Solieria filiformis lectin (rSfL)

spinqualitylabelsall models 7umj, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7umj is a 1 chain structure with sequence from Solieria filiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.88Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LEC1_SOLFI Publication Abstract from PubMed The SfL-1 isoform from the marine red algae Solieria filiformis was produced in recombinant form (rSfL-1) and showed hemagglutinating activity and inhibition similar to native SfL. The analysis of circular dichroism revealed the predominance of beta-strands structures with spectra of betaI-proteins for both lectins, which had Melting Temperature (Tm) between 41 degrees C and 53 degrees C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two beta-barrel domains formed by five antiparallel beta chains linked by a short peptide between the beta-barrels. SfL and rSfL-1 were able to agglutinate strains of Escherichia coli and Staphylococcus aureus and did not show antibacterial activity. However, SfL induced a reduction in E. coli biomass at concentrations from 250 to 125 mug mL(-1), whereas rSfL-1 induced reduction in all concentrations tested. Additionally, rSfL-1 at concentrations from 250 to 62.5 mug mL(-1), showed a statistically significant reduction in the number of colony-forming units, which was not noticed for SfL. Wound healing assay showed that the treatments with SfL and rSfL-1 act in reducing the inflammatory response and in the activation and proliferation of fibroblasts by a larger and fast deposition of collagen. Structural study and antimicrobial and wound healing effects of lectin from Solieria filiformis (Kutzing) P.W.Gabrielson.,Chaves RP, Dos Santos AKB, Andrade AL, Pinheiro AA, Silva JMS, da Silva FMS, de Sousa JP, Barroso Neto IL, Bezerra EHS, Abreu JO, de Carvalho FCT, de Sousa OV, de Sousa BL, da Rocha BAM, Silva ALC, do Nascimento Neto LG, de Vasconcelos MA, Teixeira EH, Carneiro RF, Sampaio AH, Nagano CS Biochimie. 2023 Jun 8;214(Pt B):61-76. doi: 10.1016/j.biochi.2023.05.016. PMID:37301421 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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