7E7T

Crystal structure of RSL mutant in complex with sugar Ligand

Summary for 7E7T

• Entry DOI: 10.2210/pdb7e7t/pdb
• Descriptor: Fucose-binding lectin protein,Fucose-binding lectin protein,Fucose-binding lectin protein, 2-[2-[4-[[(2R,3S,4R,5S,6S)-6-methyl-3,4,5-tris(oxidanyl)oxan-2-yl]oxymethyl]-1,2,3-triazol-1-yl]ethoxy]ethyl 2-[3,6-bis(diethylamino)-9H-xanthen-9-yl]benzoate (3 entities in total)
• Functional Keywords: complex, lectin, fucose, rhodamine, sugar binding protein
• Biological source: Ralstonia solanacearum (Pseudomonas solanacearum); More
• Total number of polymer chains: 2
• Total formula weight: 62742.46

Authors

Li, L.,Chen, G.S. (deposition date: 2021-02-27, release date: 2021-04-14, Last modification date: 2026-07-29)

Primary citation

Li, L.,Li, Z.,Wang, Z.,Chen, S.,Liu, R.,Xu, X.,Zhang, Z.,Ye, L.,Ding, Y.,Luo, Q.,Cao, S.,Zhang, L.,Imberty, A.,Chen, G.
Spatiotemporal Landscape for the Sophisticated Transformation of Protein Assemblies Defined by Multiple Supramolecular Interactions.
Acs Nano, 17:15001-15011, 2023

PubMed Abstract: Precise protein assemblies not only constitute a series of living machineries but also provide an advanced class of biomaterials. Previously, we developed the inducing ligand strategy to generate various fixed protein assemblies, without the formation of noncovalent interactions between proteins. Here, we demonstrated that controlling the symmetry and number of supramolecular interactions introduced on protein surfaces could direct the formation of unspecific interactions between proteins and induce various nanoscale assemblies, including coiling nanowires, nanotubes, and nanosheets, without manipulation of the protein's native surfaces. More importantly, these nanoscale assemblies could spontaneously evolve into more ordered architectures, crystals. We further showed that the transformation from the introduced supramolecular interactions to the interactions formed between proteins was crucial for pathway selection and outcomes of evolution. These findings reveal a transformation mechanism of protein self-assembly that has not been exploited before and may provide an approach to generate complex and transformable biomacromolecular self-assemblies.

PubMed: 37459282
DOI: 10.1021/acsnano.3c04029

Experimental method

X-RAY DIFFRACTION (1.98 Å)