1nb1
High resolution solution structure of kalata B1
OverviewOverview
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 StructureAbout this Structure
1NB1 is a Single protein structure of sequence from Oldenlandia affinis. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 02:18:58 2008