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1rpo
From Proteopedia
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(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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Revision as of 23:39, 20 November 2007
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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
Page seeded by OCA on Wed Nov 21 01:46:43 2007
