7UMJ
Crystal structure of recombinant Solieria filiformis lectin (rSfL)
This is a non-PDB format compatible entry.
Summary for 7UMJ
Entry DOI | 10.2210/pdb7umj/pdb |
Descriptor | Lectin SfL-1, SULFATE ION (3 entities in total) |
Functional Keywords | lectin, red algae, solieria filiformis, sugar binding protein |
Biological source | Solieria filiformis |
Total number of polymer chains | 1 |
Total formula weight | 30765.10 |
Authors | Chaves, R.P.,Bezerra, E.H.S.,da Silva, F.M.S.,Carneiro, R.F.,Sampaio, A.H.,Rocha, B.A.M.,Nagano, C.S. (deposition date: 2022-04-07, release date: 2023-10-11) |
Primary citation | Chaves, R.P.,Dos Santos, A.K.B.,Andrade, A.L.,Pinheiro, A.A.,Silva, J.M.S.,da Silva, F.M.S.,de Sousa, J.P.,Barroso Neto, I.L.,Bezerra, E.H.S.,Abreu, J.O.,de Carvalho, F.C.T.,de Sousa, O.V.,de Sousa, B.L.,da Rocha, B.A.M.,Silva, A.L.C.,do Nascimento Neto, L.G.,de Vasconcelos, M.A.,Teixeira, E.H.,Carneiro, R.F.,Sampaio, A.H.,Nagano, C.S. Structural study and antimicrobial and wound healing effects of lectin from Solieria filiformis (Kutzing) P.W.Gabrielson. Biochimie, 214:61-76, 2023 Cited by PubMed Abstract: 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 β-strands structures with spectra of βI-proteins for both lectins, which had Melting Temperature (Tm) between 41 °C and 53 °C. The three-dimensional structure of the rSfL-1 was determined by X-ray crystallography, revealing that it is composed of two β-barrel domains formed by five antiparallel β chains linked by a short peptide between the β-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 μg mL, whereas rSfL-1 induced reduction in all concentrations tested. Additionally, rSfL-1 at concentrations from 250 to 62.5 μg mL, 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. PubMed: 37301421DOI: 10.1016/j.biochi.2023.05.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
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