1orc

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(New page: 200px<br /><applet load="1orc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orc, resolution 1.54&Aring;" /> '''CRO REPRESSOR INSERT...)
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[[Image:1orc.gif|left|200px]]<br /><applet load="1orc" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1orc.gif|left|200px]]<br /><applet load="1orc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1orc, resolution 1.54&Aring;" />
caption="1orc, resolution 1.54&Aring;" />
'''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]'''<br />
'''CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]'''<br />
==Overview==
==Overview==
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A rationally designed, genetically engineered, monomeric form of the Cro, protein from bacteriophage lambda has been crystallized and its structure, determined by isomorphous replacement and refined to a resolution of 1.54, A. The structure confirms the rationale of the design but, at the same, time, reveals 1-2 A shifts throughout the monomer structure relative to, the previously determined structure of the dimeric wild-type protein., These changes include a 1.6 A main-chain shift in part of the beta-sheet, region of the molecule relative to the alpha-helical region and a 1.1 A, shift of a buried phenylalanine within the core as well as a correlated, 2.2 A shift in a solvent-exposed beta-hairpin. The conformational, adjustments appear to reflect an inherent flexibility of the protein that, is associated with its DNA-binding function.
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A rationally designed, genetically engineered, monomeric form of the Cro protein from bacteriophage lambda has been crystallized and its structure determined by isomorphous replacement and refined to a resolution of 1.54 A. The structure confirms the rationale of the design but, at the same time, reveals 1-2 A shifts throughout the monomer structure relative to the previously determined structure of the dimeric wild-type protein. These changes include a 1.6 A main-chain shift in part of the beta-sheet region of the molecule relative to the alpha-helical region and a 1.1 A shift of a buried phenylalanine within the core as well as a correlated 2.2 A shift in a solvent-exposed beta-hairpin. The conformational adjustments appear to reflect an inherent flexibility of the protein that is associated with its DNA-binding function.
==About this Structure==
==About this Structure==
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1ORC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ORC OCA].
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1ORC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORC OCA].
==Reference==
==Reference==
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[[Category: Enterobacteria phage lambda]]
[[Category: Enterobacteria phage lambda]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Albright, R.A.]]
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[[Category: Albright, R A.]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews, B W.]]
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[[Category: Mossing, M.C.]]
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[[Category: Mossing, M C.]]
[[Category: gene regulating protein]]
[[Category: gene regulating protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:07:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:43 2008''

Revision as of 12:20, 21 February 2008


1orc, resolution 1.54Å

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CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]

Overview

A rationally designed, genetically engineered, monomeric form of the Cro protein from bacteriophage lambda has been crystallized and its structure determined by isomorphous replacement and refined to a resolution of 1.54 A. The structure confirms the rationale of the design but, at the same time, reveals 1-2 A shifts throughout the monomer structure relative to the previously determined structure of the dimeric wild-type protein. These changes include a 1.6 A main-chain shift in part of the beta-sheet region of the molecule relative to the alpha-helical region and a 1.1 A shift of a buried phenylalanine within the core as well as a correlated 2.2 A shift in a solvent-exposed beta-hairpin. The conformational adjustments appear to reflect an inherent flexibility of the protein that is associated with its DNA-binding function.

About this Structure

1ORC is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer., Albright RA, Mossing MC, Matthews BW, Biochemistry. 1996 Jan 23;35(3):735-42. PMID:8547253

Page seeded by OCA on Thu Feb 21 14:20:43 2008

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