1wn4
From Proteopedia
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[[Image:1wn4.jpg|left|200px]] | [[Image:1wn4.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_1wn4| PDB=1wn4 | SCENE= }} | |
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'''NMR Structure of VoNTR''' | '''NMR Structure of VoNTR''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WN4 OCA]. | |
==Reference== | ==Reference== | ||
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15328347 15328347] | Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15328347 15328347] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Anderson, M A.]] | [[Category: Anderson, M A.]] | ||
[[Category: Clark, R J.]] | [[Category: Clark, R J.]] | ||
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[[Category: Renda, R F.]] | [[Category: Renda, R F.]] | ||
[[Category: Waine, C.]] | [[Category: Waine, C.]] | ||
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Revision as of 10:54, 3 May 2008
NMR Structure of VoNTR
Overview
The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis. Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved alpha-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.
About this Structure
Full crystallographic information is available from OCA.
Reference
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:15328347 Page seeded by OCA on Sat May 3 13:54:04 2008
