1wn4 | pdb_00001wn4

NMR Structure of VoNTR

spinqualitylabelsall models 1wn4, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1wn4 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1wn8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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