1JVX

Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal

1JVX の概要

• エントリーDOI: 10.2210/pdb1jvx/pdb
• 関連するPDBエントリー: 1JVY 1MDQ
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: maltodextrin-binding protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: intermolecular, cross-link, disulfide, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P02928
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41293.78

構造登録者

Srinivasan, U.,Iyer, G.H.,Przybycien, T.A.,Samsonoff, W.A.,Bell, J.A. (登録日: 2001-08-31, 公開日: 2001-09-12, 最終更新日: 2023-08-16)

主引用文献

Srinivasan, U.,Iyer, G.H.,Przybycien, T.A.,Samsonoff, W.A.,Bell, J.A.
Crystine: Fibrous Biomolecular Material from Protein Crystals Cross-linked in a Specific Geometry
Protein Eng., 15:895-902, 2002

PubMed Abstract: Cysteine substitutions were engineered on the surface of maltose binding protein to produce crystine fibers, linear polymers of folded protein formed within a crystal. Disulfide bond formation between adjacent protein molecules within the lattice was monitored by X-ray crystallography. The cross-linked crystals were resistant to dissolution in water or neutral buffer solutions, even though the cross-linking was one-dimensional. However, crystine fibers were observed by transmission electron microscopy to dissociate from the crystals in acidic solutions. Some fibers remained associated as two-dimensional bundles or sheets, with a repeat unit along the fibers consistent with the packing of the individual protein molecules in the crystal. Neutralization of the acidic solutions caused the fibers to re-associate as a solid. Crystine threads were drawn out of this solution. In scanning electron microscopy images, many individual fibers could be seen unwinding from the ends of some threads. Crystine fibers are a new type of biomolecular material with potential applications wherever the use of proteins in a fibrous form is desirable, for example, the incorporation of enzymes into cloth or filtration material.

PubMed: 12538909
DOI: 10.1093/protein/15.11.895

実験手法

X-RAY DIFFRACTION (2.5 Å)