1rzs
From Proteopedia
(New page: 200px<br /><applet load="1rzs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzs" /> '''Solution structure of P22 Cro'''<br /> ==Ov...) |
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| - | [[Image:1rzs.gif|left|200px]]<br /><applet load="1rzs" size=" | + | [[Image:1rzs.gif|left|200px]]<br /><applet load="1rzs" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of P22 Cro'''<br /> | '''Solution structure of P22 Cro'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the solution structure of the Cro protein from bacteriophage | + | We report the solution structure of the Cro protein from bacteriophage P22. Comparisons of its sequence and structure to those of lambda Cro strongly suggest an alpha-to-beta secondary structure switching event during Cro evolution. The folds of P22 Cro and lambda Cro share a three alpha helix fragment comprising the N-terminal half of the domain. However, P22 Cro's C terminus folds as two helices, while lambda Cro's folds as a beta hairpin. The all-alpha fold found for P22 Cro appears to be ancestral, since it also occurs in cI proteins, which are anciently duplicated paralogues of Cro. PSI-BLAST and transitive homology analyses strongly suggest that the sequences of P22 Cro and lambda Cro are globally homologous despite encoding different folds. The alpha+beta fold of lambda Cro therefore likely evolved from its all-alpha ancestor by homologous secondary structure switching, rather than by nonhomologous replacement of both sequence and structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1RZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http:// | + | 1RZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
| - | [[Category: Cordes, M | + | [[Category: Cordes, M H.]] |
| - | [[Category: Konieczka, J | + | [[Category: Konieczka, J H.]] |
[[Category: Newlove, T.]] | [[Category: Newlove, T.]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
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[[Category: structural evolution]] | [[Category: structural evolution]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:31 2008'' |
Revision as of 12:56, 21 February 2008
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Solution structure of P22 Cro
Overview
We report the solution structure of the Cro protein from bacteriophage P22. Comparisons of its sequence and structure to those of lambda Cro strongly suggest an alpha-to-beta secondary structure switching event during Cro evolution. The folds of P22 Cro and lambda Cro share a three alpha helix fragment comprising the N-terminal half of the domain. However, P22 Cro's C terminus folds as two helices, while lambda Cro's folds as a beta hairpin. The all-alpha fold found for P22 Cro appears to be ancestral, since it also occurs in cI proteins, which are anciently duplicated paralogues of Cro. PSI-BLAST and transitive homology analyses strongly suggest that the sequences of P22 Cro and lambda Cro are globally homologous despite encoding different folds. The alpha+beta fold of lambda Cro therefore likely evolved from its all-alpha ancestor by homologous secondary structure switching, rather than by nonhomologous replacement of both sequence and structure.
About this Structure
1RZS is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Secondary structure switching in Cro protein evolution., Newlove T, Konieczka JH, Cordes MH, Structure. 2004 Apr;12(4):569-81. PMID:15062080
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