2ih0
From Proteopedia
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'''NMR structure determination of a synthetic analogue of the iturinic antibiotic bacillomycin Lc''' | '''NMR structure determination of a synthetic analogue of the iturinic antibiotic bacillomycin Lc''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IH0 OCA]. | |
==Reference== | ==Reference== | ||
NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics., Volpon L, Tsan P, Majer Z, Vass E, Hollosi M, Noguera V, Lancelin JM, Besson F, Spectrochim Acta A Mol Biomol Spectrosc. 2007 Aug;67(5):1374-81. Epub 2006, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17129757 17129757] | NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics., Volpon L, Tsan P, Majer Z, Vass E, Hollosi M, Noguera V, Lancelin JM, Besson F, Spectrochim Acta A Mol Biomol Spectrosc. 2007 Aug;67(5):1374-81. Epub 2006, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17129757 17129757] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Besson, F.]] | [[Category: Besson, F.]] | ||
[[Category: Lancelin, J.]] | [[Category: Lancelin, J.]] | ||
[[Category: Tsan, P.]] | [[Category: Tsan, P.]] | ||
[[Category: Volpon, L.]] | [[Category: Volpon, L.]] | ||
| - | [[Category: | + | [[Category: Bacillomycin lc]] |
| - | [[Category: | + | [[Category: Cyclopeptide]] |
| - | [[Category: | + | [[Category: Iturin]] |
| - | [[Category: | + | [[Category: Synthetic peptide]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:29:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:29, 4 May 2008
NMR structure determination of a synthetic analogue of the iturinic antibiotic bacillomycin Lc
Overview
Iturins are a group of antifungal produced by Bacillus subtilis. All are cyclic lipopeptides with seven alpha-amino acids of configuration LDDLLDL and one beta-amino fatty acid. The bacillomycin L is a member of this family and its NMR structure was previously resolved using the sequence Asp-Tyr-Asn-Ser-Gln-Ser-Thr. In this work, we carefully examined the NMR spectra of this compound and detected an error in the sequence. In fact, Asp1 and Gln5 need to be changed into Asn1 and Glu5, which therefore makes it identical to bacillomycin Lc. As a consequence, it now appears that all iturinic peptides with antibiotic activity share the common beta-amino fatty acid 8-L-Asn1-D-Tyr2-D-Asn3 sequence. To better understand the conformational influence of the acidic residue L-Asp1, present, for example in the inactive iturin C, the NMR structure of the synthetic analogue SCP [cyclo (L-Asp1-D-Tyr2-D-Asn3-L-Ser4-L-Gln5-D-Ser6-L-Thr7-beta-Ala8)] was determined and compared with bacillomycin Lc recalculated with the corrected sequence. In both cases, the conformers obtained were separated into two families of similar energy which essentially differ in the number and type of turns. A detailed analysis of both cyclopeptide structures is presented here. In addition, CD and FTIR spectra were performed and confirmed the conformational differences observed by NMR between both cyclopeptides.
About this Structure
Full crystallographic information is available from OCA.
Reference
NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics., Volpon L, Tsan P, Majer Z, Vass E, Hollosi M, Noguera V, Lancelin JM, Besson F, Spectrochim Acta A Mol Biomol Spectrosc. 2007 Aug;67(5):1374-81. Epub 2006, Oct 19. PMID:17129757 Page seeded by OCA on Sun May 4 07:29:33 2008
