2eir
From Proteopedia
(New page: 200px<br /><applet load="2eir" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eir, resolution 2.50Å" /> '''Design of Disulfide-...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2eir.jpg|left|200px]]<br /><applet load="2eir" size=" | + | [[Image:2eir.jpg|left|200px]]<br /><applet load="2eir" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2eir, resolution 2.50Å" /> | caption="2eir, resolution 2.50Å" /> | ||
'''Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts'''<br /> | '''Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2EIR 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 CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2EIR 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=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EIR OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:48:37 2008'' |
Revision as of 10:48, 23 January 2008
|
Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts
Overview
Disulfide bonds play an important role in protein stability and function., Here, we describe a general procedure for generating disulfide-linked, dimers and multimers of proteins of known crystal structures. An algorithm, was developed to predict sites in a protein compatible with intermolecular, disulfide formation with neighboring molecules in the crystal lattice. A, database analysis was carried out on 46 PDB coordinates to verify the, general applicability of this algorithm to predict intermolecular, disulfide linkages. On the basis of the predictions from this algorithm, mutants were constructed and characterized for a model protein, thioredoxin. Of the five mutants, as predicted, in solution four formed, disulfide-linked dimers while one formed polymers. Thermal and chemical, denaturation studies on these mutant thioredoxins showed that three of the, four dimeric mutants had similar stability to wild-type thioredoxin while, one had lower stability. Three of the mutant dimers crystallized readily, (in four to seven days) in contrast to the wild-type protein, which is, particularly difficult to crystallize and takes more than a month to form, diffraction-quality crystals. In two of the three cases, the structure of, the dimer was exactly as predicted by the algorithm, while in the third, case the relative orientation of the monomers in the dimer was different, from the predicted one. This methodology can be used to enhance protein, crystallizability, modulate the oligomerization state and to produce, linear chains or ordered three-dimensional protein arrays.
About this Structure
2EIR is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts., Das M, Kobayashi M, Yamada Y, Sreeramulu S, Ramakrishnan C, Wakatsuki S, Kato R, Varadarajan R, J Mol Biol. 2007 Aug 2;. PMID:17727880
Page seeded by OCA on Wed Jan 23 12:48:37 2008
