1rpo
From Proteopedia
(New page: 200px<br /><applet load="1rpo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpo, resolution 1.4Å" /> '''RESTORED HEPTAD PATTE...) |
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| - | [[Image:1rpo.jpg|left|200px]]<br /><applet load="1rpo" size=" | + | [[Image:1rpo.jpg|left|200px]]<br /><applet load="1rpo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rpo, resolution 1.4Å" /> | caption="1rpo, resolution 1.4Å" /> | ||
'''RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE'''<br /> | '''RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The sequences of alpha-helical coiled-coils and bundles are characterized | + | The sequences of alpha-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frequently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour. Thus, formation of alpha-alpha-hairpin bends may occur both in the presence and absence of heptad breaks. |
==About this Structure== | ==About this Structure== | ||
| - | 1RPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1RPO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1RPO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:18 2008'' |
Revision as of 12:53, 21 February 2008
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RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE
Overview
The sequences of alpha-helical coiled-coils and bundles are characterized by a specific pattern of hydrophobic and hydrophilic residues which is repeated every seven residues. Highly conserved breaks in this pattern frequently occur in segments of otherwise continuous heptad substructures. The hairpin bend of the ROP protein coincides with such a break and provides a model system for the study of the structural effects induced by heptad discontinuities. The structure of a ROP mutant which re-establishes a continuous heptad pattern, shows insignificant changes relative to the wild-type protein, as is also reflected in its conformational stability, spectroscopic properties and unfolding behaviour. Thus, formation of alpha-alpha-hairpin bends may occur both in the presence and absence of heptad breaks.
About this Structure
1RPO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Restored heptad pattern continuity does not alter the folding of a four-alpha-helix bundle., Vlassi M, Steif C, Weber P, Tsernoglou D, Wilson KS, Hinz HJ, Kokkinidis M, Nat Struct Biol. 1994 Oct;1(10):706-16. PMID:7634075
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