1JVX
Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal
Summary for 1JVX
Entry DOI | 10.2210/pdb1jvx/pdb |
Related | 1JVY 1MDQ |
Related PRD ID | PRD_900001 |
Descriptor | maltodextrin-binding protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
Functional Keywords | intermolecular, cross-link, disulfide, transport protein |
Biological source | Escherichia coli |
Cellular location | Periplasm: P02928 |
Total number of polymer chains | 1 |
Total formula weight | 41293.78 |
Authors | Srinivasan, U.,Iyer, G.H.,Przybycien, T.A.,Samsonoff, W.A.,Bell, J.A. (deposition date: 2001-08-31, release date: 2001-09-12, Last modification date: 2023-08-16) |
Primary citation | 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 Cited by 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: 12538909DOI: 10.1093/protein/15.11.895 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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