5T7P

Crystal structure of Pisum arvense lectin (PAL) complexed with X-Man

5T7P の概要

• エントリーDOI: 10.2210/pdb5t7p/pdb
• 分子名称: Lectin, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: pisum arvense, lectin, pal, x-man., sugar binding protein
• 由来する生物種: Pisum sativum (Garden pea)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53046.52

構造登録者

Pinto-Junior, V.R.,Santiago, M.Q.,Osterne, V.J.S.,Silva-Filho, J.C.,Rocha, B.A.M.,Delatorre, P.,Nascimento, K.S.,Cavada, B.S. (登録日: 2016-09-05, 公開日: 2017-08-09, 最終更新日: 2023-10-04)

主引用文献

Pinto-Junior, V.R.,Santiago, M.Q.,Nobre, C.B.,Osterne, V.J.S.,Leal, R.B.,Cajazeiras, J.B.,Lossio, C.F.,Rocha, B.A.M.,Martins, M.G.Q.,Nobre, C.A.S.,Silva, M.T.L.,Nascimento, K.S.,Cavada, B.S.
Crystal structure of Pisum arvense seed lectin (PAL) and characterization of its interaction with carbohydrates by molecular docking and dynamics.
Arch. Biochem. Biophys., 630:27-37, 2017

PubMed Abstract: The Pisum arvense lectin (PAL), a legume protein belonging to the Vicieae tribe, is capable of specific recognition of mannose, glucose and its derivatives without altering its structure. In this work, the three-dimensional structure of PAL was determined by X-ray crystallography and studied in detail by a combination of molecular docking and molecular dynamics (MD). Crystals belonging to monoclinic space group P2 were grown by the vapor diffusion method at 293 K. The structure was solved at 2.16 Å and was similar to that of other Vicieae lectins. The structure presented R and R of 17.04% and 22.08%, respectively, with all acceptable geometric parameters. Molecular docking was performed to analyze interactions of the lectin with monosaccharides, disaccharides and high-mannose N-glycans. PAL demonstrated different affinities on carbohydrates, depending on bond orientation and glycosidic linkage present in ligands. Furthermore, the lectin interacted with representative N-glycans in a manner consistent with the biological effects described for Vicieae lectins. Carbohydrate-recognition domain (CRD) in-depth analysis was performed by MD, describing the behavior of CRD residues in complex with ligand, stability, flexibility of the protein over time, CRD volume and topology. This is a first report of its kind for a lectin of the Vicieae tribe.

PubMed: 28754321
DOI: 10.1016/j.abb.2017.07.013

実験手法

X-RAY DIFFRACTION (2.16 Å)