1nbj
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(New page: 200px<br /><applet load="1nbj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nbj" /> '''High-resolution solution structure of cyclov...)
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Revision as of 19:59, 20 November 2007
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High-resolution solution structure of cycloviolacin O1
Overview
In recent years an increasing number of miniproteins containing an, amide-cyclized backbone have been discovered. The cyclotide family is the, largest group of such proteins and is characterized by a circular protein, backbone and six conserved cysteine residues linked by disulfide bonds in, a tight core of the molecule. These form a cystine knot in which an, embedded ring formed by two of the disulfide bonds and the connecting, backbone segment is threaded by a third disulfide bond. In the current, study we have undertaken high resolution structural analysis of two, prototypic cyclotides, kalata B1 and cycloviolacin O1, to define the role, of the conserved residues in the sequence. We provide the first, comprehensive analysis of the topological features in this unique family, of proteins, namely rings (a circular backbone), twists (a cis-peptide, bond in the Mobius cyclotides) and knots (a knotted arrangement of the, disulfide bonds).
About this Structure
1NBJ is a Single protein structure of sequence from Viola odorata. Full crystallographic information is available from OCA.
Reference
Twists, knots, and rings in proteins. Structural definition of the cyclotide framework., Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ, J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:12482868
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