1iyc
From Proteopedia
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[[Image:1iyc.jpg|left|200px]] | [[Image:1iyc.jpg|left|200px]] | ||
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'''Solution structure of antifungal peptide, scarabaecin''' | '''Solution structure of antifungal peptide, scarabaecin''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IYC is a [[Single protein]] structure | + | 1IYC is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Tomie, T.]] | [[Category: Tomie, T.]] | ||
[[Category: Yamakawa, M.]] | [[Category: Yamakawa, M.]] | ||
| - | [[Category: | + | [[Category: Antifungal peptide]] |
| - | [[Category: | + | [[Category: Antimicrobial peptide]] |
| - | [[Category: | + | [[Category: Beetle]] |
| - | [[Category: | + | [[Category: Chitin-binding]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:34:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:34, 2 May 2008
Solution structure of antifungal peptide, scarabaecin
Overview
Scarabaecin isolated from hemolymph of the coconut rhinoceros beetle Oryctes rhinoceros is a 36-residue polypeptide that has antifungal activity. The solution structure of scarabaecin has been determined from twodimensional 1H NMR spectroscopic data and hybrid distance geometry-simulated annealing protocol calculation. Based on 492 interproton and 10 hydrogen-bonding distance restraints and 36 dihedral angle restraints, we obtained 20 structures. The average backbone root-mean-square deviation for residues 4-35 is 0.728 +/- 0.217 A from the mean structure. The solution structure consists of a two-stranded antiparallel beta-sheet connected by a type-I beta-turn after a short helical turn. All secondary structures and a conserved disulfide bond are located in the C-terminal half of the peptide, residues 18-36. Overall folding is stabilized by a combination of a disulfide bond, seven hydrogen bonds, and numerous hydrophobic interactions. The structural motif of the C-terminal half shares a significant tertiary structural similarity with chitin-binding domains of plant and invertebrate chitin-binding proteins, even though scarabaecin has no overall sequence similarity to other peptide/polypeptides including chitin-binding proteins. The length of its primary structure, the number of disulfide bonds, and the pattern of conserved functional residues binding to chitin in scarabaecin differ from those of chitin-binding proteins in other invertebrates and plants, suggesting that scarabaecin does not share a common ancestor with them. These results are thought to provide further strong experimental evidence to the hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.
About this Structure
1IYC is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros., Hemmi H, Ishibashi J, Tomie T, Yamakawa M, J Biol Chem. 2003 Jun 20;278(25):22820-7. Epub 2003 Apr 3. PMID:12676931 Page seeded by OCA on Fri May 2 20:34:41 2008
