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PDBsum entry 1vb8
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Plant protein PDB id
1vb8

 

 

 

 

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Contents
Protein chain
30 a.a.
PDB id:
1vb8
Name: Plant protein
Title: Solution structure of vhr1, the first cyclotide from root tissue
Structure: Viola hederacea root peptide 1. Chain: a. Synonym: vhr1
Source: Viola hederacea. Organism_taxid: 180952. Tissue: roots
NMR struc: 20 models
Authors: M.Trabi,D.J.Craik
Key ref: M.Trabi and D.J.Craik (2004). Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1. Plant Cell, 16, 2204-2216. PubMed id: 15295104
Date:
25-Feb-04     Release date:   21-Dec-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P83937  (VHR1_VIOHE) -  Root cyclotide 1 from Viola hederacea
Seq:
Struc: 		30 a.a.
30 a.a.
Key:    PfamA domain  Secondary structure

 

 
Plant Cell 16:2204-2216 (2004)
PubMed id: 15295104  
 
 
Tissue-specific expression of head-to-tail cyclized miniproteins in Violaceae and structure determination of the root cyclotide Viola hederacea root cyclotide1.
M.Trabi, D.J.Craik.
 
  ABSTRACT  
 
The plant cyclotides are a family of 28 to 37 amino acid miniproteins characterized by their head-to-tail cyclized peptide backbone and six absolutely conserved Cys residues arranged in a cystine knot motif: two disulfide bonds and the connecting backbone segments form a loop that is penetrated by the third disulfide bond. This knotted disulfide arrangement, together with the cyclic peptide backbone, renders the cyclotides extremely stable against enzymatic digest as well as thermal degradation, making them interesting targets for both pharmaceutical and agrochemical applications. We have examined the expression patterns of these fascinating peptides in various Viola species (Violaceae). All tissue types examined contained complex mixtures of cyclotides, with individual profiles differing significantly. We provide evidence for at least 57 novel cyclotides present in a single Viola species (Viola hederacea). Furthermore, we have isolated one cyclotide expressed only in underground parts of V. hederacea and characterized its primary and three-dimensional structure. We propose that cyclotides constitute a new family of plant defense peptides, which might constitute an even larger and, in their biological function, more diverse family than the well-known plant defensins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21337607 R.G.Ovesen, K.K.Brandt, U.Göransson, J.Nielsen, H.C.Hansen, and N.Cedergreen (2011).
Biomedicine in the environment: Cyclotides constitute potent natural toxins in plants and soil bacteria.
  Environ Toxicol Chem, 30, 1190-1196.  
20835453 L.Cascales, and D.J.Craik (2010).
Naturally occurring circular proteins: distribution, biosynthesis and evolution.
  Org Biomol Chem, 8, 5035-5047.  
19211551 C.K.Wang, S.H.Hu, J.L.Martin, T.Sjögren, J.Hajdu, L.Bohlin, P.Claeson, U.Göransson, K.J.Rosengren, J.Tang, N.H.Tan, and D.J.Craik (2009).
Combined X-ray and NMR analysis of the stability of the cyclotide cystine knot fold that underpins its insecticidal activity and potential use as a drug scaffold.
  J Biol Chem, 284, 10672-10683.
PDB codes: 2k7g 3e4h
19423383 D.J.Craik (2009).
Circling the enemy: cyclic proteins in plant defence.
  Trends Plant Sci, 14, 328-335.  
19462049 M.Trabi, J.S.Mylne, L.Sando, and D.J.Craik (2009).
Circular proteins from Melicytus (Violaceae) refine the conserved protein and gene architecture of cyclotides.
  Org Biomol Chem, 7, 2378-2388.  
18438714 H.Dörnenburg (2008).
Plant cell culture technology-harnessing a biological approach for competitive cyclotides production.
  Biotechnol Lett, 30, 1311-1321.  
18385853 P.Thongyoo, N.Roqué-Rosell, R.J.Leatherbarrow, and E.W.Tate (2008).
Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides.
  Org Biomol Chem, 6, 1462-1470.  
18058973 T.Leta Aboye, R.J.Clark, D.J.Craik, and U.Göransson (2008).
Ultra-stable peptide scaffolds for protein engineering-synthesis and folding of the circular cystine knotted cyclotide cycloviolacin O2.
  Chembiochem, 9, 103-113.  
17372654 D.J.Craik, and N.L.Daly (2007).
NMR as a tool for elucidating the structures of circular and knotted proteins.
  Mol Biosyst, 3, 257-265.  
17534989 M.R.Plan, U.Göransson, R.J.Clark, N.L.Daly, M.L.Colgrave, and D.J.Craik (2007).
The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides.
  Chembiochem, 8, 1001-1011.  
16440288 D.J.Craik, M.Cemazar, C.K.Wang, and N.L.Daly (2006).
The cyclotide family of circular miniproteins: nature's combinatorial peptide template.
  Biopolymers, 84, 250-266.  
15893660 J.P.Mulvenna, L.Sando, and D.J.Craik (2005).
Processing of a 22 kDa precursor protein to produce the circular protein tricyclon A.
  Structure, 13, 691-701.
PDB code: 1yp8
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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