4GU8

Crystal Structure of Burkholderia oklahomensis agglutinin (BOA)

4GU8 の概要

• エントリーDOI: 10.2210/pdb4gu8/pdb
• 関連するPDBエントリー: 4GK9
• 分子名称: Burkholderia oklahomensis agglutinin (BOA), GLYCEROL, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (4 entities in total)
• 機能のキーワード: lectin, sugar binding, beta barrel, anti-hiv, man9, glycan, gp120, sugar binding protein
• 由来する生物種: Burkholderia oklahomensis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 233029.42

構造登録者

Whitley, M.J.,Furey, W.,Gronenborn, A.M. (登録日: 2012-08-29, 公開日: 2013-05-08, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)