1u9p
From Proteopedia
(New page: 200px<br /><applet load="1u9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u9p, resolution 1.9Å" /> '''Permuted single-chain...) |
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| - | [[Image:1u9p.gif|left|200px]]<br /><applet load="1u9p" size=" | + | [[Image:1u9p.gif|left|200px]]<br /><applet load="1u9p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u9p, resolution 1.9Å" /> | caption="1u9p, resolution 1.9Å" /> | ||
'''Permuted single-chain Arc'''<br /> | '''Permuted single-chain Arc'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We designed a single-chain variant of the Arc repressor homodimer in which | + | We designed a single-chain variant of the Arc repressor homodimer in which the beta strands that contact operator DNA are connected by a hairpin turn and the alpha helices that form the tetrahelical scaffold of the dimer are attached by a short linker. The designed protein represents a noncyclic permutation of secondary structural elements in another single-chain Arc molecule (Arc-L1-Arc), in which the two subunits are fused by a single linker. The permuted protein binds operator DNA with nanomolar affinity, refolds on the sub-millisecond time scale, and is as stable as Arc-L1-Arc. The crystal structure of the permuted protein reveals an essentially wild-type fold, demonstrating that crucial folding information is not encoded in the wild-type order of secondary structure. Noncyclic rearrangement of secondary structure may allow grouping of critical active-site residues in other proteins and could be a useful tool for protein design and minimization. |
==About this Structure== | ==About this Structure== | ||
| - | 1U9P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1U9P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1U9P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Cezairliyan, B | + | [[Category: Cezairliyan, B O.]] |
| - | [[Category: Cochrane, J | + | [[Category: Cochrane, J C.]] |
| - | [[Category: Grant, R | + | [[Category: Grant, R A.]] |
| - | [[Category: Sauer, R | + | [[Category: Sauer, R T.]] |
| - | [[Category: Tabtiang, R | + | [[Category: Tabtiang, R K.]] |
[[Category: arc]] | [[Category: arc]] | ||
[[Category: parc]] | [[Category: parc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:08 2008'' |
Revision as of 13:22, 21 February 2008
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Permuted single-chain Arc
Overview
We designed a single-chain variant of the Arc repressor homodimer in which the beta strands that contact operator DNA are connected by a hairpin turn and the alpha helices that form the tetrahelical scaffold of the dimer are attached by a short linker. The designed protein represents a noncyclic permutation of secondary structural elements in another single-chain Arc molecule (Arc-L1-Arc), in which the two subunits are fused by a single linker. The permuted protein binds operator DNA with nanomolar affinity, refolds on the sub-millisecond time scale, and is as stable as Arc-L1-Arc. The crystal structure of the permuted protein reveals an essentially wild-type fold, demonstrating that crucial folding information is not encoded in the wild-type order of secondary structure. Noncyclic rearrangement of secondary structure may allow grouping of critical active-site residues in other proteins and could be a useful tool for protein design and minimization.
About this Structure
1U9P is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Consolidating critical binding determinants by noncyclic rearrangement of protein secondary structure., Tabtiang RK, Cezairliyan BO, Grant RA, Cochrane JC, Sauer RT, Proc Natl Acad Sci U S A. 2005 Feb 15;102(7):2305-9. Epub 2005 Feb 2. PMID:15689399
Page seeded by OCA on Thu Feb 21 15:22:08 2008
