1nbj
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1nbj.gif|left|200px]] | + | [[Image:1nbj.gif|left|200px]] |
| - | + | ||
| - | '''High-resolution solution structure of cycloviolacin O1''' | + | {{Structure |
| + | |PDB= 1nbj |SIZE=350|CAPTION= <scene name='initialview01'>1nbj</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''High-resolution solution structure of cycloviolacin O1''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1NBJ is a [ | + | 1NBJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Viola_odorata Viola odorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBJ OCA]. |
==Reference== | ==Reference== | ||
| - | Twists, knots, and rings in proteins. Structural definition of the cyclotide framework., Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ, J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:[http:// | + | Twists, knots, and rings in proteins. Structural definition of the cyclotide framework., Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ, J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12482868 12482868] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Viola odorata]] | [[Category: Viola odorata]] | ||
| Line 23: | Line 32: | ||
[[Category: cystine knot]] | [[Category: cystine knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:39 2008'' |
Revision as of 10:54, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
High-resolution solution structure of cycloviolacin O1
Overview
In recent years an increasing number of miniproteins containing an amide-cyclized backbone have been discovered. The cyclotide family is the largest group of such proteins and is characterized by a circular protein backbone and six conserved cysteine residues linked by disulfide bonds in a tight core of the molecule. These form a cystine knot in which an embedded ring formed by two of the disulfide bonds and the connecting backbone segment is threaded by a third disulfide bond. In the current study we have undertaken high resolution structural analysis of two prototypic cyclotides, kalata B1 and cycloviolacin O1, to define the role of the conserved residues in the sequence. We provide the first comprehensive analysis of the topological features in this unique family of proteins, namely rings (a circular backbone), twists (a cis-peptide bond in the Mobius cyclotides) and knots (a knotted arrangement of the disulfide bonds).
About this Structure
1NBJ is a Single protein structure of sequence from Viola odorata. Full crystallographic information is available from OCA.
Reference
Twists, knots, and rings in proteins. Structural definition of the cyclotide framework., Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ, J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:12482868
Page seeded by OCA on Thu Mar 20 12:54:39 2008
