1wn8
From Proteopedia
(New page: 200px<br /><applet load="1wn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wn8" /> '''NMR Structure of OaNTR'''<br /> ==Overview=...) |
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| - | [[Image:1wn8.jpg|left|200px]]<br /><applet load="1wn8" size=" | + | [[Image:1wn8.jpg|left|200px]]<br /><applet load="1wn8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wn8" /> | caption="1wn8" /> | ||
'''NMR Structure of OaNTR'''<br /> | '''NMR Structure of OaNTR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The cyclotides are the largest family of naturally occurring circular | + | 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== | ==About this Structure== | ||
| - | 1WN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1WN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WN8 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15328347 15328347] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, M | + | [[Category: Anderson, M A.]] |
| - | [[Category: Clark, R | + | [[Category: Clark, R J.]] |
| - | [[Category: Craik, D | + | [[Category: Craik, D J.]] |
| - | [[Category: Daly, N | + | [[Category: Daly, N L.]] |
| - | [[Category: Dutton, J | + | [[Category: Dutton, J L.]] |
| - | [[Category: Jennings, C | + | [[Category: Jennings, C V.]] |
| - | [[Category: Renda, R | + | [[Category: Renda, R F.]] |
[[Category: Waine, C.]] | [[Category: Waine, C.]] | ||
[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:15 2008'' |
Revision as of 13:46, 21 February 2008
|
NMR Structure of OaNTR
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
1WN8 is a Single protein structure of sequence from [1]. 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 Thu Feb 21 15:46:15 2008
