4GK9

Crystal structure of Burkholderia oklahomensis agglutinin (BOA) bound to 3a,6a-mannopentaose

Summary for 4GK9

• Entry DOI: 10.2210/pdb4gk9/pdb
• Descriptor: agglutinin (BOA), alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose, SODIUM ION, ... (5 entities in total)
• Functional Keywords: lectin, sugar binding, beta barrel, anti-hiv, man9, glycan, gp120, sugar binding protein
• Biological source: Burkholderia oklahomensis
• Total number of polymer chains: 1
• Total formula weight: 32458.79

Authors

Whitley, M.J.,Furey, W.,Gronenborn, A.M. (deposition date: 2012-08-10, release date: 2013-05-08, Last modification date: 2024-02-28)

Primary citation

Whitley, M.J.,Furey, W.,Kollipara, S.,Gronenborn, A.M.
Burkholderia oklahomensis agglutinin is a canonical two-domain OAA-family lectin: structures, carbohydrate binding and anti-HIV activity.
Febs J., 280:2056-2067, 2013

PubMed Abstract: Burkholderia oklahomensis EO147 agglutinin (BOA) is a 29 kDa member of the Oscillatoria agardhii agglutinin (OAA) family of lectins. Members of the OAA family recognize high-mannose glycans, and, by binding to the HIV envelope glycoprotein 120 (gp120), block the virus from binding to and entering the host cell, thereby inhibiting infection. OAA-family lectins comprise either one or two homologous domains, with a single domain possessing two glycan binding sites. We solved the structure of BOA in the ligand-free form as well as in complex with four molecules of 3α,6α-mannopentaose, the core unit of the N-linked high-mannose structures found on gp120 in vivo. This is the first structure of a double-domain OAA-family lectin in which all four binding sites are occupied by ligand. The structural details of the BOA-glycan interactions presented here, together with determination of affinity constants and HIV inactivation data, shed further light onto the structure-function relationship in this important class of anti-HIV proteins.

PubMed: 23480609
DOI: 10.1111/febs.12229

Experimental method

X-RAY DIFFRACTION (1.9 Å)