3OBL

Crystal structure of the potent anti-HIV cyanobacterial lectin from Oscillatoria Agardhii

Summary for 3OBL

• Entry DOI: 10.2210/pdb3obl/pdb
• Descriptor: Lectin, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (3 entities in total)
• Functional Keywords: novel beta barrel fold, anti-hiv lectin, high mannose glycans, sugar binding protein
• Biological source: Planktothrix agardhii (Oscillatoria agardhii)
• Total number of polymer chains: 2
• Total formula weight: 28746.78

Authors

Koharudin, L.M.I.,Furey, W.,Gronenborn, A.M. (deposition date: 2010-08-06, release date: 2010-10-20, Last modification date: 2024-02-21)

Primary citation

Koharudin, L.M.,Furey, W.,Gronenborn, A.M.
Novel fold and carbohydrate specificity of the potent anti-HIV cyanobacterial lectin from Oscillatoria agardhii.
J.Biol.Chem., 286:1588-1597, 2011

PubMed Abstract: Oscillatoria agardhii agglutinin (OAA) is a recently discovered cyanobacterial lectin that exhibits potent anti-HIV activity. Up to now, only its primary structure and carbohydrate binding data have been available. To elucidate the structural basis for the antiviral mechanism of OAA, we determined the structure of this lectin by x-ray crystallography at 1.2 Å resolution and mapped the specific carbohydrate recognition sites of OAA by NMR spectroscopy. The overall architecture of OAA comprises 10 β-strands that fold into a single, compact, β-barrel-like domain, creating a unique topology compared with all known protein structures in the Protein Data Bank. OAA sugar binding was tested against Man-9 and various disaccharide components of Man-9. Two symmetric carbohydrate-binding sites were located on the protein, and a preference for Manα(1-6)Man-linked sugars was found. Altogether, our structural results explain the antiviral activity OAA and add to the growing body of knowledge about antiviral lectins.

PubMed: 20961847
DOI: 10.1074/jbc.M110.173278

Experimental method

X-RAY DIFFRACTION (1.2 Å)