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| | {{STRUCTURE_1n1u| PDB=1n1u | SCENE= }} | | {{STRUCTURE_1n1u| PDB=1n1u | SCENE= }} |
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| - | '''NMR structure of [Ala1,15]kalata B1'''
| + | ===NMR structure of [Ala1,15]kalata B1=== |
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| - | ==Overview==
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| - | The plant cyclotides are a fascinating family of circular proteins that contain a cyclic cystine knot motif. The knotted topology and cyclic nature of the cyclotides pose interesting questions about folding mechanisms and how the knotted arrangement of disulfide bonds is formed. In the current study we have examined the oxidative refolding and reductive unfolding of the prototypic cyclotide, kalata B1. A stable two-disulfide intermediate accumulated during oxidative refolding but not in reductive unfolding. Mass spectrometry and NMR spectroscopy were used to show that the intermediate contained a native-like structure with two native disulfide bonds topologically similar to the intermediate isolated for the related cystine knot protein EETI-II (Le-Nguyen, D., Heitz, A., Chiche, L., El Hajji, M., and Castro B. (1993) Protein Sci. 2, 165-174). However, the folding intermediate observed for kalata B1 is not the immediate precursor of the three-disulfide native peptide and does not accumulate in the reductive unfolding process, in contrast to the intermediate observed for EETI-II. These alternative pathways of linear and cyclic cystine knot proteins appear to be related to the constraints imposed by the cyclic backbone of kalata B1 and the different ring size of the cystine knot. The three-dimensional structure of a synthetic version of the two-disulfide intermediate of kalata B1 in which Ala residues replace the reduced Cys residues provides a structural insight into why the two-disulfide intermediate is a kinetic trap on the folding pathway. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12482862}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12482862 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12482862}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1N1U is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1U OCA]. | + | 1N1U is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1U OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Cystine knot]] | | [[Category: Cystine knot]] |
| | [[Category: Triple stranded beta sheet]] | | [[Category: Triple stranded beta sheet]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:59:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:03:02 2008'' |
Revision as of 02:03, 28 July 2008
Template:STRUCTURE 1n1u
NMR structure of [Ala1,15]kalata B1
Template:ABSTRACT PUBMED 12482862
About this Structure
1N1U is a Single protein structure. Full experimental information is available from OCA.
Reference
Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides., Daly NL, Clark RJ, Craik DJ, J Biol Chem. 2003 Feb 21;278(8):6314-22. Epub 2002 Dec 12. PMID:12482862
Page seeded by OCA on Mon Jul 28 05:03:02 2008
