1NB1
High resolution solution structure of kalata B1
Summary for 1NB1
| Entry DOI | 10.2210/pdb1nb1/pdb |
| Related | 1KAL |
| Descriptor | kalata B1 (1 entity in total) |
| Functional Keywords | cyclotide, cyclic backbone, cystine knot, cck, insecticidal, antibiotic |
| Biological source | Oldenlandia affinis |
| Total number of polymer chains | 1 |
| Total formula weight | 2917.34 |
| Authors | Rosengren, K.J.,Daly, N.L.,Plan, M.R.,Waine, C.,Craik, D.J. (deposition date: 2002-12-01, release date: 2003-03-18, Last modification date: 2024-10-23) |
| Primary citation | Rosengren, K.J.,Daly, N.L.,Plan, M.R.,Waine, C.,Craik, D.J. Twists, Knots, and Rings in Proteins. STRUCTURAL DEFINITION OF THE CYCLOTIDE FRAMEWORK J.Biol.Chem., 278:8606-8616, 2003 Cited by PubMed Abstract: 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 Möbius cyclotides) and knots (a knotted arrangement of the disulfide bonds). PubMed: 12482868DOI: 10.1074/jbc.M211147200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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