1WN4
NMR Structure of VoNTR
Summary for 1WN4
| Entry DOI | 10.2210/pdb1wn4/pdb |
| Related | 1WN8 |
| Descriptor | VoNTR protein (1 entity in total) |
| Functional Keywords | helix, plant protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2963.43 |
| Authors | Dutton, J.L.,Renda, R.F.,Waine, C.,Clark, R.J.,Daly, N.L.,Jennings, C.V.,Anderson, M.A.,Craik, D.J. (deposition date: 2004-07-27, release date: 2004-09-14, Last modification date: 2024-05-29) |
| Primary citation | Dutton, J.L.,Renda, R.F.,Waine, C.,Clark, R.J.,Daly, N.L.,Jennings, C.V.,Anderson, M.A.,Craik, D.J. Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins J.Biol.Chem., 279:46858-46867, 2004 Cited by PubMed Abstract: 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. PubMed: 15328347DOI: 10.1074/jbc.M407421200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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