1jvx: Difference between revisions
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[[Image:1jvx.gif|left|200px]] | [[Image:1jvx.gif|left|200px]] | ||
'''Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal''' | {{Structure | ||
|PDB= 1jvx |SIZE=350|CAPTION= <scene name='initialview01'>1jvx</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene> | |||
|ACTIVITY= | |||
|GENE= malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JVX is a [ | 1JVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12538909 12538909] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: intermolecular]] | [[Category: intermolecular]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:13 2008'' | ||
Revision as of 13:09, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | malE (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal
OverviewOverview
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 StructureAbout this Structure
1JVX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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