1X1V

Structure Of Banana Lectin- Methyl-Alpha-Mannose Complex

1X1V の概要

• エントリーDOI: 10.2210/pdb1x1v/pdb
• 分子名称: lectin, methyl alpha-D-mannopyranoside, ZINC ION, ... (5 entities in total)
• 機能のキーワード: all beta sheet protein, beta prism-i fold, mannose specific, sugar binding protein
• 由来する生物種: Musa acuminata
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31243.17

構造登録者

Singh, D.D.,Saikrishnan, K.,Kumar, P.,Surolia, A.,Sekar, K.,Vijayan, M. (登録日: 2005-04-14, 公開日: 2005-11-08, 最終更新日: 2023-10-25)

主引用文献

Singh, D.D.,Saikrishnan, K.,Kumar, P.,Surolia, A.,Sekar, K.,Vijayan, M.
Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies
Glycobiology, 15:1025-1032, 2005

PubMed Abstract: The crystal structure of a complex of methyl-alpha-D-mannoside with banana lectin from Musa paradisiaca reveals two primary binding sites in the lectin, unlike in other lectins with beta-prism I fold which essentially consists of three Greek key motifs. It has been suggested that the fold evolved through successive gene duplication and fusion of an ancestral Greek key motif. In other lectins, all from dicots, the primary binding site exists on one of the three motifs in the three-fold symmetric molecule. Banana is a monocot, and the three motifs have not diverged enough to obliterate sequence similarity among them. Two Greek key motifs in it carry one primary binding site each. A common secondary binding site exists on the third Greek key. Modelling shows that both the primary sites can support 1-2, 1-3, and 1-6 linked mannosides with the second residue interacting in each case primarily with the secondary binding site. Modelling also readily leads to a bound branched mannopentose with the nonreducing ends of the two branches anchored at the two primary binding sites, providing a structural explanation for the lectin's specificity for branched alpha-mannans. A comparison of the dimeric banana lectin with other beta-prism I fold lectins, provides interesting insights into the variability in their quaternary structure.

PubMed: 15958419
DOI: 10.1093/glycob/cwi087

実験手法

X-RAY DIFFRACTION (2.45 Å)