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Structural and biochemical characteristics of the cyclotide kalata B5 from Oldenlandia affinis.
Univ Queensland, Div Chem & Struct Biol, Inst Mol Biosci, St Lucia, Qld 4067 Australia.
Univ Queensland, Div Chem & Struct Biol, Inst Mol Biosci, St Lucia, Qld 4067 Australia. (BBCL)
Univ Queensland, Div Chem & Struct Biol, Inst Mol Biosci, St Lucia, Qld 4067 Australia.
Univ Queensland, Div Chem & Struct Biol, Inst Mol Biosci, St Lucia, Qld 4067 Australia.
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2010 (English)In: Biopolymers, ISSN 0006-3525, E-ISSN 1097-0282, Vol. 94, no 5, Sp. Iss. SI, 647-658 p.Article in journal (Refereed) Published
Abstract [en]

Cyclotides are a large family of plant-derived proteins typified by their head-to-tail cyclic backbone and knotted arrangement of three disulfide bonds. Although they display a diverse range of biological activities, their native function is thought to be plant defense. Here we characterized the expression, three-dimensional structure, and hemolytic activity of the cyclotide kalata B5 from the African plant Oldenlandia affinis. Kalata B5 shows an interesting seasonal variation in its expression and can only be isolated during certain times of the year, when the plant is flowering. It displays a typical tightly folded cyclic cystine knot structure. A range of pH and temperature titrations reveal that a conserved glutamic acid in loop 1 of the structure forms a key hydrogen bond network, similar to that reported previously for other cyclotides. However, specific line broadening in the NMR spectra of kalata B5 suggests that the hydrogen bonding network in this peptide is less rigid than in other cyclotides. Notably, the pK(a) of Glu6 of 4.5 is higher than the values for other cyclotides studied so far, which range from 3.0 to 4.0, providing a further indication of a weaker hydrogen bond network. Kalata B5 has only moderate hemolytic activity compared with other highly expressed cyclotides, and this reduced activity probably reflects its more flexible structure. As is the case with other cyclotides, kalata B5 has an exposed hydrophobic region on its surface, supporting suggestions that this hydrophobic patch is a key feature for membrane binding and biological activity of cyclotides. (c) 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2010.

Place, publisher, year, edition, pages
2010. Vol. 94, no 5, Sp. Iss. SI, 647-658 p.
Identifiers
URN: urn:nbn:se:lnu:diva-7753DOI: 10.1002/bip.21409PubMedID: 20564013OAI: oai:DiVA.org:lnu-7753DiVA: diva2:345237
Note

Symposium on Biopolymers Peptide Science held at Ist International Conference on Circular Proteins Queens Isl, AUSTRALIA, OCT, 2009

Available from: 2010-08-24 Created: 2010-08-24 Last updated: 2017-02-07Bibliographically approved

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