7dc0

Crystal structure of glycan-free Pseudomonas taiwanensis lectin

spinqualitylabelsall models 7dc0, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7dc0 is a 2 chain structure with sequence from Pseudomonas taiwanensis DSM 21245. 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 A0A2L1HSZ4_9PSED Publication Abstract from PubMed Homologues of the Oscillatoria agardhii agglutinin (OAA) lectins contain a sequence repeat of approximately 66 amino acids, with the number of tandem repeats varying across family members. OAA homologues bind high-mannose glycans on viral surface proteins, thereby interfering with viral entry into host cells. As such, OAA homologues have potential utility as antiviral agents, but a more detailed understanding of their structure-function relationships would enable us to develop improved constructs. Here, we determined the X-ray crystal structure of free and glycan-bound forms of Pseudomonas taiwanensis lectin (PTL), an OAA-family lectin consisting of two tandem repeats. Like other OAA-family lectins, PTL exhibited a beta-barrel-like structure with two symmetrically positioned glycan-binding sites at the opposite ends of the barrel. Upon glycan binding, the conformation of PTL undergoes a more significant change than expected from previous OAA structural analysis. Moreover, the electron density of the bound glycans suggested that the binding affinities are different at the two binding sites. Next, based on analysis of these structures, we used site-specific mutagenesis to create PTL constructs expected to increase the population with a conformation suitable for glycan binding. The engineered PTLs were examined for their antiviral activity against the influenza virus. Interestingly, some exhibited stronger activity compared with that of the parent PTL. We propose that our approach is effective for the generation of potential microbicides with enhanced antiviral activity. Lectins engineered to favor a glycan-binding conformation have enhanced antiviral activity.,Matoba Y, Sato Y, Oda K, Hatori Y, Morimoto K J Biol Chem. 2021 Apr 22:100698. doi: 10.1016/j.jbc.2021.100698. PMID:33895142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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