The N-terminal pro-domain of the kalata B1 cyclotide precursor is intrinsically unstructured

Daly, Norelle L., Gunasekera, Sunithi, Clark, Richard J., Lin, Feng, Wade, John D., Anderson, Marilyn and Craik, David J. (2016) The N-terminal pro-domain of the kalata B1 cyclotide precursor is intrinsically unstructured. Biopolymers, 106 6: 825-833. doi:10.1002/bip.22977


Author Daly, Norelle L.
Gunasekera, Sunithi
Clark, Richard J.
Lin, Feng
Wade, John D.
Anderson, Marilyn
Craik, David J.
Title The N-terminal pro-domain of the kalata B1 cyclotide precursor is intrinsically unstructured
Journal name Biopolymers   Check publisher's open access policy
ISSN 1097-0282
Publication date 2016-08-26
Sub-type Article (original research)
DOI 10.1002/bip.22977
Open Access Status Not yet assessed
Volume 106
Issue 6
Start page 825
End page 833
Total pages 25
Place of publication Hoboken, NJ, United States
Publisher John Wiley & Sons
Language eng
Formatted abstract
Cyclotides are plant-derived, gene-encoded, circular peptides with a range of host-defense functions, including insecticidal activity. They also have potential as pharmaceutical scaffolds and understanding their biosynthesis is important to facilitate their large-scale production. Insights into the biosynthesis of cyclotides are emerging but there are still open questions, particularly regarding the influence of the structure of the precursor proteins on processing/biosynthetic pathways. The precursor protein of kalata B1, encoded by the plant Oldenlandia affinis, contains N- and C-terminal propeptides that flank the mature cyclotide domain. The C-terminal region (ctr) is important for the cyclization process, whereas the N-terminal repeat (ntr) has been implicated in vacuolar targeting. In this study we examined the structure and folding of various truncated constructs of the ntr coupled to the mature domain of kalata B1. Despite the ntr having a well-defined helical structure in isolation, once coupled to the natively folded mature domain there is no evidence of an ordered structure. Surprisingly, the ntr appears to be highly disordered and induces self-association of the precursor. This self-association might be associated with the role of the ntr as a vacuolar-targeting signal, as previously shown for unrelated storage proteins.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Accepted Manuscript. Published online 26 August 2016

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
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Created: Fri, 09 Sep 2016, 22:12:57 EST by Susan Allen on behalf of Institute for Molecular Bioscience