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3N3H

Erythrina corallodendron lectin mutant (Y106G) in complex with citrate

3N3H の概要
エントリーDOI10.2210/pdb3n3h/pdb
関連するPDBエントリー1AX0 1AX1 1FYU 1SFY 3N35 3N36
分子名称Lectin, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
機能のキーワードlegume lectin, glycosylation, erythrina lectin, sugar, recombinant lectin, sugar binding protein
由来する生物種Erythrina corallodendron (coral tree)
タンパク質・核酸の鎖数1
化学式量合計26779.50
構造登録者
Thamotharan, S.,Karthikeyan, T.,Kulkarni, K.A.,Shetty, K.N.,Surolia, A.,Vijayan, M.,Suguna, K. (登録日: 2010-05-20, 公開日: 2011-03-30, 最終更新日: 2023-11-01)
主引用文献Thamotharan, S.,Karthikeyan, T.,Kulkarni, K.A.,Shetty, K.N.,Surolia, A.,Vijayan, M.,Suguna, K.
Modification of the sugar specificity of a plant lectin: structural studies on a point mutant of Erythrina corallodendron lectin.
Acta Crystallogr.,Sect.D, 67:218-227, 2011
Cited by
PubMed Abstract: A mutant of Erythrina corallodendron lectin was generated with the aim of enhancing its affinity for N-acetylgalactosamine. A tyrosine residue close to the binding site of the lectin was mutated to a glycine in order to facilitate stronger interactions between the acetamido group of the sugar and the lectin which were prevented by the side chain of the tyrosine in the wild-type lectin. The crystal structures of this Y106G mutant lectin in complex with galactose and N-acetylgalactosamine have been determined. A structural rationale has been provided for the differences in the relative binding affinities of the wild-type and mutant lectins towards the two sugars based on the structures. A hydrogen bond between the O6 atom of the sugars and the variable loop of the carbohydrate-binding site of the lectin is lost in the mutant complexes owing to a conformational change in the loop. This loss is compensated by an additional hydrogen bond that is formed between the acetamido group of the sugar and the mutant lectin in the complex with N-acetylgalactosamine, resulting in a higher affinity of the mutant lectin for N-acetylgalactosamine compared with that for galactose, in contrast to the almost equal affinity of the wild-type lectin for the two sugars. The structure of a complex of the mutant with a citrate ion bound at the carbohydrate-binding site that was obtained while attempting to crystallize the complexes with sugars is also presented.
PubMed: 21358053
DOI: 10.1107/S0907444911004525
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 3n3h
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-16に公開中

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