2CHH

RALSTONIA SOLANACEARUM HIGH-AFFINITY MANNOSE-BINDING LECTIN

「1VYY」から置き換えられました

2CHH の概要

• エントリーDOI: 10.2210/pdb2chh/pdb
• 関連するPDBエントリー: 1UQX
• 分子名称: PROTEIN RSC3288, CALCIUM ION, UNKNOWN ATOM OR ION, ... (6 entities in total)
• 機能のキーワード: lectin, sugar-binding protein, d-mannose, plant pathogen, hypothetical protein
• 由来する生物種: RALSTONIA SOLANACEARUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12179.46

構造登録者

Mitchell, E.P.,Wimmerova, M.,Imberty, A. (登録日: 2006-03-15, 公開日: 2006-03-16, 最終更新日: 2023-12-13)

主引用文献

Sudakevitz, D.,Kostlanova, N.,Blatman-Jan, G.,Mitchell, E.P.,Lerrer, B.,Wimmerova, M.,Katcoff, D.J.,Imberty, A.,Gilboa-Garber, N.
A new Ralstonia solanacearum high-affinity mannose-binding lectin RS-IIL structurally resembling the Pseudomonas aeruginosa fucose-specific lectin PA-IIL.
Mol. Microbiol., 52:691-700, 2004

PubMed Abstract: The plant pathogen Ralstonia solanacearum produces two lectins, each with different affinity to fucose. We described previously the properties and sequence of the first lectin, RSL (subunit M(r) 9.9 kDa), which is related to fungal lectins (Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., 2002, J Biochem 132: 353-358). The present communication reports the discovery of the second one, RS-IIL (subunit M(r) 11.6 kDa), a tetrameric lectin, with high sequence similarity to the fucose-binding lectin PA-IIL of Pseudomonas aeruginosa. RS-IIL recognizes fucose but displays much higher affinity to mannose and fructose, which is opposite to the preference spectrum of PA-IIL. Determination of the crystal structure of RS-IIL complexed with a mannose derivative demonstrates a tetrameric structure very similar to the recently solved PA-IIL structure (Mitchell, E., et al., 2002, Nature Struct Biol 9: 918-921). Each monomer contains two close calcium cations that mediate the binding of the monosaccharide and explain the outstandingly high affinity to the monosaccharide ligand. The binding loop of the cations is fully conserved in RS-IIL and PA-IIL, whereas the preference for mannose versus fucose can be attributed to the change of a three-amino-acid sequence in the 'specificity loop'.

PubMed: 15101976
DOI: 10.1111/j.1365-2958.2004.04020.x

実験手法

X-RAY DIFFRACTION (1 Å)