1SFY
Crystal structure of recombinant Erythrina corallodandron Lectin
1SFY の概要
| エントリーDOI | 10.2210/pdb1sfy/pdb |
| 関連するPDBエントリー | 1AX0 1FYU |
| 関連するBIRD辞書のPRD_ID | PRD_900004 |
| 分子名称 | Lectin, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total) |
| 機能のキーワード | legume lectin, glycosylation, erythrina lectin, sugar binding protein |
| 由来する生物種 | Erythrina corallodendron |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 160233.04 |
| 構造登録者 | Kulkarni, K.A.,Srivastava, A.,Mitra, N.,Surolia, A.,Vijayan, M.,Suguna, K. (登録日: 2004-02-21, 公開日: 2004-08-10, 最終更新日: 2023-10-25) |
| 主引用文献 | Kulkarni, K.A.,Srivastava, A.,Mitra, N.,Sharon, N.,Surolia, A.,Vijayan, M.,Suguna, K. Effect of glycosylation on the structure of Erythrina corallodendron lectin. Proteins, 56:821-827, 2004 Cited by PubMed Abstract: The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non-covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate specificity of the lectin. The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation. PubMed: 15281133DOI: 10.1002/prot.20168 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.55 Å) |
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