1y66
From Proteopedia
(New page: 200px<br /><applet load="1y66" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y66, resolution 1.65Å" /> '''Dioxane contributes ...) |
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| - | [[Image:1y66.gif|left|200px]]<br /><applet load="1y66" size=" | + | [[Image:1y66.gif|left|200px]]<br /><applet load="1y66" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1y66, resolution 1.65Å" /> | caption="1y66, resolution 1.65Å" /> | ||
'''Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant'''<br /> | '''Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Our goal was to compute a stable, full-sequence design of the Drosophila | + | Our goal was to compute a stable, full-sequence design of the Drosophila melanogaster engrailed homeodomain. Thermal and chemical denaturation data indicated the design was significantly more stable than was the wild-type protein. The data were also nearly identical to those for a similar, later full-sequence design, which was shown by NMR to adopt the homeodomain fold: a three-helix, globular monomer. However, a 1.65 A crystal structure of the design described here turned out to be of a completely different fold: a four-helix, rodlike tetramer. The crystallization conditions included approximately 25% dioxane, and subsequent experiments by circular dichroism and sedimentation velocity analytical ultracentrifugation indicated that dioxane increases the helicity and oligomerization state of the designed protein. We attribute at least part of the discrepancy between the target fold and the crystal structure to the presence of a high concentration of dioxane. |
==About this Structure== | ==About this Structure== | ||
| - | 1Y66 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CD, DIO and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Y66 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CD:'>CD</scene>, <scene name='pdbligand=DIO:'>DIO</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y66 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hom, G | + | [[Category: Hom, G K.]] |
| - | [[Category: Lassila, J | + | [[Category: Lassila, J K.]] |
| - | [[Category: Mayo, S | + | [[Category: Mayo, S L.]] |
| - | [[Category: Thomas, L | + | [[Category: Thomas, L M.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: protein design]] | [[Category: protein design]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:07 2008'' |
Revision as of 14:02, 21 February 2008
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Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant
Overview
Our goal was to compute a stable, full-sequence design of the Drosophila melanogaster engrailed homeodomain. Thermal and chemical denaturation data indicated the design was significantly more stable than was the wild-type protein. The data were also nearly identical to those for a similar, later full-sequence design, which was shown by NMR to adopt the homeodomain fold: a three-helix, globular monomer. However, a 1.65 A crystal structure of the design described here turned out to be of a completely different fold: a four-helix, rodlike tetramer. The crystallization conditions included approximately 25% dioxane, and subsequent experiments by circular dichroism and sedimentation velocity analytical ultracentrifugation indicated that dioxane increases the helicity and oligomerization state of the designed protein. We attribute at least part of the discrepancy between the target fold and the crystal structure to the presence of a high concentration of dioxane.
About this Structure
1Y66 is a Protein complex structure of sequences from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant., Hom GK, Lassila JK, Thomas LM, Mayo SL, Protein Sci. 2005 Apr;14(4):1115-9. Epub 2005 Mar 1. PMID:15741348
Page seeded by OCA on Thu Feb 21 16:02:07 2008
Categories: Escherichia coli | Protein complex | Hom, G K. | Lassila, J K. | Mayo, S L. | Thomas, L M. | ACY | CD | DIO | Dioxane | Engrailed homeodomain | Protein design
