This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1jvy
From Proteopedia
(New page: 200px<br /><applet load="1jvy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jvy, resolution 1.90Å" /> '''Maltodextrin-binding...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1jvy.gif|left|200px]]<br /><applet load="1jvy" size=" | + | [[Image:1jvy.gif|left|200px]]<br /><applet load="1jvy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jvy, resolution 1.90Å" /> | caption="1jvy, resolution 1.90Å" /> | ||
'''Maltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides'''<br /> | '''Maltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cysteine substitutions were engineered on the surface of maltose binding | + | 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== | ==About this Structure== | ||
| - | 1JVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MAL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MAL:'>MAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVY OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bell, J | + | [[Category: Bell, J A.]] |
| - | [[Category: Iyer, G | + | [[Category: Iyer, G H.]] |
| - | [[Category: Przybycien, T | + | [[Category: Przybycien, T A.]] |
| - | [[Category: Samsonoff, W | + | [[Category: Samsonoff, W A.]] |
[[Category: Srinivasan, U.]] | [[Category: Srinivasan, U.]] | ||
[[Category: MAL]] | [[Category: MAL]] | ||
| Line 23: | Line 23: | ||
[[Category: intermolecular]] | [[Category: intermolecular]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:21 2008'' |
Revision as of 11:27, 21 February 2008
|
Maltodextrin-binding protein variant D207C/A301GS/P316C with beta-mercaptoethanol mixed disulfides
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
1JVY is a Single protein structure of sequence from Escherichia coli with 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 Thu Feb 21 13:27:21 2008
