1jvx
From Proteopedia
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Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal
Overview
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.
About this Structure
1JVX is a Single protein structure of sequence from Escherichia coli with MAL as ligand. Full crystallographic information is available from OCA.
Reference
Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry., Srinivasan U, Iyer GH, Przybycien TA, Samsonoff WA, Bell JA, Protein Eng. 2002 Nov;15(11):895-902. PMID:12538909
Page seeded by OCA on Tue Nov 20 18:37:19 2007
