1jvx: Difference between revisions

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[[Image:1jvx.gif|left|200px]]
[[Image:1jvx.gif|left|200px]]


{{Structure
<!--
|PDB= 1jvx |SIZE=350|CAPTION= <scene name='initialview01'>1jvx</scene>, resolution 2.50&Aring;
The line below this paragraph, containing "STRUCTURE_1jvx", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
-->
|DOMAIN=
{{STRUCTURE_1jvx|  PDB=1jvx |  SCENE= }}  
|RELATEDENTRY=[[1mdq|1MDQ]], [[1jvy|1JVY]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvx OCA], [http://www.ebi.ac.uk/pdbsum/1jvx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jvx RCSB]</span>
}}


'''Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal'''
'''Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal'''
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[[Category: Samsonoff, W A.]]
[[Category: Samsonoff, W A.]]
[[Category: Srinivasan, U.]]
[[Category: Srinivasan, U.]]
[[Category: cross-link]]
[[Category: Cross-link]]
[[Category: disulfide]]
[[Category: Disulfide]]
[[Category: intermolecular]]
[[Category: Intermolecular]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:59:33 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:39:46 2008''

Revision as of 21:59, 2 May 2008

File:1jvx.gif

Template:STRUCTURE 1jvx

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 Page seeded by OCA on Fri May 2 21:59:33 2008

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